Abstract
Long interspersed element-1 (LINE-1 or L1) retrotransposons represent the only functional family of autonomous transposable elements in humans and formed 17% of our genome. Even though most of the human L1 sequences are inactive, a limited number of copies per individual retain the ability to mobilize by a process termed retrotransposition. The ongoing L1 retrotransposition may result in insertional mutagenesis that could lead to negative consequences such as genetic disease and cancer. For this reason, cells have evolved several mechanisms of defense to restrict L1 activity. Among them, a critical role for cellular deaminases [activation-induced deaminase (AID)/apolipoprotein B mRNA-editing catalytic polypeptide-like (APOBEC) and adenosine deaminases that act on RNA (ADAR) enzymes] has emerged. The majority of the AID/APOBEC family of proteins are responsible for the deamination of cytosine to uracil (C-to-U editing) within DNA and RNA targets. The ADARs convert adenosine bases to inosines (A-to-I editing) within double-stranded RNA (dsRNA) targets. This review will discuss the current understanding of the regulation of LINE-1 retrotransposition mediated by these enzymes.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Aktaş T, Avşar Ilık İ, Maticzka D, Bhardwaj V, Pessoa Rodrigues C, Mittler G, Manke T, Backofen R, Akhtar A (2017) DHX9 suppresses RNA processing defects originating from the Alu invasion of the human genome. Nature 544:115–119. https://doi.org/10.1038/nature21715
Anwar F, Davenport MP, Ebrahimi D (2013) Footprint of APOBEC3 on the genome of human retroelements. J Virol 87:8195–8204. https://doi.org/10.1128/JVI.00298-13
Aravin AA, Sachidanandam R, Bourc’his D, Schaefer C, Pezic D, Toth KF et al (2008) A piRNA pathway primed by individual transposons is linked to de novo DNA methylation in mice. Mol Cell 31:785–799. https://doi.org/10.1016/j.molcel.2008.09.003
Bass BL (2002) RNA editing by adenosine deaminases that act on RNA. Annu Rev Biochem 71:817–846. https://doi.org/10.1146/annurev.biochem.71.110601.135501
Bass BL, Weintraub H (1987) A developmentally regulated activity that unwinds RNA duplexes. Cell 48:607–613
Bass BL, Weintraub H (1988) An unwinding activity that covalently modifies its double-stranded RNA substrate. Cell 55:1089–1098
Bass BL, Nishikura K, Keller W, Seeburg PH, Emeson RB, O’Connell MA, Samuel CE, Herbert A (1997) A standardized nomenclature for adenosine deaminases that act on RNA. RNA 3:947–949
Bazak L, Levanon EY, Eisenberg E (2014) Genome-wide analysis of Alu editability. Nucleic Acids Res 42:6876–6884. https://doi.org/10.1093/nar/gku414
Beale RC, Petersen-Mahrt SK, Watt IN, Harris RS, Rada C, Neuberger MS (2004) Comparison of the differential context-dependence of DNA Deamination by APOBEC enzymes: correlation with mutation spectra in vivo. J Mol Biol 337:585–596. https://doi.org/10.1016/j.jmb.2004.01.046
Beck CR, Garcia-Perez JL, Badge RM, Moran JV (2011) LINE-1 elements in structural variation and disease. Ann Rev Genomics Hum Genet 12:187–215. https://doi.org/10.1146/annurev-genom-082509-141802
Belancio VP, Hedges DJ, Deininger P (2006) LINE-1 RNA splicing and influences on mammalian gene expression. Nucleic Acids Res 34:1512–1521. https://doi.org/10.1093/nar/gkl027
Belancio VP, Roy-Engel AM, Deininger P (2008) The impact of multiple splice sites in human L1 elements. Gene 411:38–45. https://doi.org/10.1016/j.gene.2007.12.022
Bestor TH, Bourc’his D (2004) Transposon silencing and imprint establishment in mammalian germ cells. Cold Spring Harb Symp Quant Biol 69:381–387. https://doi.org/10.1101/sqb.2004.69.381
Betts L, Xiang S, Short SA, Wolfenden R, Carter CW Jr (1994) Cytidine deaminase. The 2.3 a° crystal structure of an enzyme: transition-state analog complex. J Mol Biol 235:635–656. https://doi.org/10.1006/jmbi.1994.1018
Bogerd HP, Wiegand HL, Hulme AE, Garcia-Perez JL, O’Shea KS, Moran JV, Cullen BR (2006) Cellular inhibitors of long interspersed element 1 and Alu retrotransposition. Proc Natl Acad Sci U S A 103:8780–8785. https://doi.org/10.1073/pnas.0603313103
Branco MR, Ficz G, Reik W (2011) Uncovering the role of 5-hydroxymethylcytosine in the epigenome. Rev Genet 13:7–13. https://doi.org/10.1038/nrg3080
Bransteitter R, Pham P, Scharff MD, Goodman MF (2003) Activation-induced Cytidine Deaminase Deaminates Deoxycytidine on single-stranded DNA but requires the action of RNAse. Proc Natl Acad Sci U S A 100:4102–4107. https://doi.org/10.1073/pnas.0730835100
Brennecke J, Malone CD, Aravin AA, Sachidanandam R, Stark A, Hannon GJ (2008) An epigenetic role for maternally inherited piRNAs in transposon silencing. Science 322:1387–1392
Brouha B, Schustak J, Badge RM, Lutz-Prigge S, Farley AH, Moran JV, Kazazian HH Jr (2003) Hot L1s account for the bulk of retrotransposition in the human population. Proc Natl Acad Sci U S A 100:5280–5285. https://doi.org/10.1073/pnas.0831042100
Bulut-Karslioglu A, De La Rosa-Velázquez IA, Ramirez F, Barenboim M, Onishi-Seebacher M, Arand J et al (2014) Suv39h-dependent H3K9me3 marks intact retrotransposons and silences LINE elements in mouse embryonic stem cells. Mol Cell 55:277–290. https://doi.org/10.1016/j.molcel.2014.05.029
Burns KH (2017) Transposable elements in cancer. Nat Rev Cancer 17:415–424. https://doi.org/10.1038/nrc.2017.35
Capshew CR, Dusenbury KL, Hundley HA (2012) Inverted Alu dsRNA structures do not affect localization but can alter translation efficiency of human mRNAs independent of RNA editing. Nucleic Acids Res 40:8637–8645. https://doi.org/10.1093/nar/gks590
Chaudhuri J, Tian M, Khuong C, Chua K, Pinaud E, Alt FW (2003) Transcription-targeted DNA Deamination by the AID antibody diversification enzyme. Nature 422:726–730. https://doi.org/10.1038/nature01574
Chen LL, Carmichael GG (2012) Nuclear editing of mRNA 3-UTRs. Curr Top Microbiol Immunol 353:111–121. https://doi.org/10.1007/82_2011_149
Chen H, Lilley CE, Yu Q, Lee DV, Chou J, Narvaiza I, Landau NR, Weitzman MD (2006) APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons. Curr Biol 16:480–855. https://doi.org/10.1016/j.cub.2006.01.031
Chen KM, Harjes E, Gross PJ, Fahmy A, Lu Y, Shindo K, Harris RS, Matsuo H (2008a) Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature 452:116–119. https://doi.org/10.1038/nature06638
Chen LL, DeCerbo JN, Carmichael GG (2008b) Alu element-mediated gene silencing. EMBO J 27:1694–1705. https://doi.org/10.1038/emboj.2008.94
Chenais B, Caruso A, Hiard S, Casse N (2012) The impact of transposable elements on eukaryotic genomes: from genome size increase to genetic adaptation to stressful environments. Gene 509:7–15. https://doi.org/10.1016/j.gene.2012.07.042
Chiu YL, Greene WC (2008) The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements. Annu Rev Immunol 26:317–353. https://doi.org/10.1146/annurev.immunol.26.021607.090350
Conticello SG (2008) The AID/APOBEC family of nucleic acid mutators. Genome Biol 9:229. https://doi.org/10.1186/gb-2008-9-6-229
Conticello SG, Thomas CJ, Petersen-Mahrt SK, Neuberger MS (2005) Evolution of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases. Mol Biol Evol 22:367–377. https://doi.org/10.1093/molbev/msi026
Cost GJ, Feng Q, Jacquier A, Boeke JD (2002) Human L1 element target-primed reverse transcription in vitro. EMBO J 21:5899–5910
Coufal NG, Garcia-Perez JL, Peng GE, Yeo GW, Mu Y, Lovci MT, Morell M, O’Shea KS, Moran JV, Gage FH (2009) L1 retrotransposition in human neural progenitor cells. Nature 460:1127–1131. https://doi.org/10.1038/nature08248
Coufal NG, Garcia-Perez JL, Peng GE, Marchetto MC, Muotri AR, Mu Y, Carson CT, Macia A, Moran JV, Gage FH (2011) Ataxia telangiectasia mutated (ATM) modulates long interspersed element-1 (L1) retrotransposition in human neural stem cells. Nat Protoc 108:20382–20387. https://doi.org/10.1073/pnas.1100273108
Criscione SW, Theodosakis N, Micevic G, Cornish TC, Burns KH, Neretti N, Rodić N (2016) Genome-wide characterization of human L1 antisense promoter-driven transcripts. BMC Genomics 17:463. https://doi.org/10.1186/s12864-016-2800-5
Crow YJ, Manel N (2015) Aicardi-Goutières syndrome and the type I interferonopathies. Nat Rev Immunol 15:429–440. https://doi.org/10.1038/nri3850
Denli AM, Narvaiza I, Kerman BE, Pena M, Benner C, Marchetto MC, Diedrich JK, Aslanian A, Ma J, Moresco JJ et al (2015) Primate-specific ORF0 contributes to retrotransposon-mediated diversity. Cell 163:583–593. https://doi.org/10.1016/j.cell.2015.09.025
Dewannieux M, Esnault C, Heidmann T (2003) LINE-mediated retrotransposition of marked Alu sequences. Nat Genet 35:41–48. https://doi.org/10.1038/ng1223
Dewannieux M, Dupressoir A, Harper F, Pierron G, Heidmann T (2004) Identification of autonomous IAP LTR retrotransposons mobile in mammalian cells. Nat Genet 36:534–539
Di Noia J, Neuberger MS (2002) Altering the pathway of immunoglobulin hypermutation by inhibiting uracil-DNA glycosylase. Nature 419:43–48. https://doi.org/10.1038/nature00981
Dickerson SK, Market E, Besmer E, Papavasiliou FN (2003) AID mediates Hypermutation by Deaminating single stranded DNA. J Exp Med 197:1291–1296. https://doi.org/10.1084/jem.20030481
Doolittle WF, Sapienza C (1980) Selfish genes, the phenotype paradigm and genome evolution. Nature 284:601–603
Doria M, Neri F, Gallo A, Farace MG, Michienzi A (2009) Editing of HIV-1 RNA by the double-stranded RNA deaminase ADAR1 stimulates viral infection. Nucleic Acids Res 37:5848–5858. https://doi.org/10.1093/nar/gkp604
Doria M, Tomaselli S, Neri F, Ciafrè SA, Farace MG, Michienzi A, Gallo A (2011) ADAR2 editing enzyme is a novel human immunodeficiency virus-1 proviral factor. J Gen Virol 92:1228–1232. https://doi.org/10.1099/vir.0.028043-0
Doucet AJ, Hulme AE, Sahinovic E, Kulpa DA, Moldovan JB, Kopera HC, Athanikar JN, Hasnaoui M, Bucheton A, Moran JV, Gilbert N (2010) Characterization of LINE-1 ribonucleoprotein particles. PLoS Genet 6:e1001150. https://doi.org/10.1371/journal.pgen.1001150
Doucet-O’Hare TT, Rodić N, Sharma R, Darbari I, Abril G, Choi JA, Young Ahn J, Cheng Y, Anders RA, Burns KH, Meltzer SJ, Kazazian HH Jr (2015) LINE-1 expression and retrotransposition in Barrett’s esophagus and esophageal carcinoma. Proc Natl Acad Sci U S A 112:E4894–E4900. https://doi.org/10.1073/pnas.1502474112
Doucet-O’Hare TT, Sharma R, Rodić N, Anders RA, Burns KH, Kazazian HH Jr (2016) Somatically acquired LINE-1 insertions in normal esophagus undergo Clonal expansion in esophageal Squamous cell carcinoma. Hum Mutat 37:942–954. https://doi.org/10.1002/humu.23027
Esnault C, Maestre J, Heidmann T (2000) Human LINE retrotransposons generate processed pseudogenes. Nat Genet 24:363–367. https://doi.org/10.1038/74184
Esnault C, Heidmann O, Delebecque F, Dewannieux M, Ribet D, Hance AJ, Heidmann T, Schwartz O (2005) APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses. Nature 433:430–433. https://doi.org/10.1038/nature03238
Esnault C, Millet J, Schwartz O, Heidmann T (2006) Dual inhibitory effects of APOBEC family proteins on retrotransposition of mammalian endogenous retroviruses. Nucleic Acids Res 34:1522–1531. https://doi.org/10.1093/nar/gkl054
Feng Q, Moran JV, Kazazian HH Jr, Boeke JD (1996) Human L1 retrotransposon encodes a conserved endonuclease required for retrotransposition. Cell 87:905–916
Feng Y, Goubran MH, Follack TB, Chelico L (2017) Deamination-independent restriction of LINE-1 retrotransposition by APOBEC3H. Sci Rep 7:10881. https://doi.org/10.1038/s41598-017-11344-4
Feschotte C, Pritham EJ (2007) DNA transposons and the evolution of eukaryotic genomes. Annu Rev Genet 41:331–368. https://doi.org/10.1146/annurev.genet.40.110405.090448
Fritzell K, Xu LD, Lagergren J, Öhman M (2017) ADARs and editing: the role of A-to-I RNA modification in cancer progression. Semin Cell Dev Biol S1084-9521(17):30133–30137. https://doi.org/10.1016/j.semcdb.2017.11.018
Furukawa A, Nagata T, Matsugami A, Habu Y, Sugiyama R, Hayashi F, Kobayashi N, Yokoyama S, Takaku H, Katahira M (2009) Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G. EMBO J 28:440–451. https://doi.org/10.1038/emboj.2008.290
Gallo A, Vukic D, Michalík D, O’Connell MA, Keegan LP (2017) ADAR RNA editing in human disease; more to it than meets the I. Hum Genet 136:1265–1278. https://doi.org/10.1007/s00439-017-1837-0
Gallois-Montbrun S, Kramer B, Swanson CM, Byers H, Lynham S, Ward M, Malim MH (2007) Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules. J Virol 81:2165–2178. https://doi.org/10.1128/JVI.02287-06
Garcia-Perez JL, Marchetto MC, Muotri AR, Coufal NG, Gage FH, O’Shea KS, Moran JV (2007) LINE-1 retrotransposition in human embryonic stem cells. Hum Mol Genet 16:1569–1577. https://doi.org/10.1093/hmg/ddm105
George CX, Ramaswami G, Li JB, Samuel CE (2016) Editing of cellular self-RNAs by adenosine deaminase ADAR1 suppresses innate immune stress responses. J Biol Chem 291:6158–6168. https://doi.org/10.1074/jbc.M115.709014
Gerber AP, Keller W (1999) An adenosine deaminase that generates inosine at the wobble position of tRNAs. Science 286:1146–1149
Gerber AP, Keller W (2001) RNA editing by base deamination: more enzymes, more targets, newmysteries. Trends Biochem Sci 26:376–384
Goodier JL (2016) Restricting retrotransposons: a review. Mob DNA 7:16. https://doi.org/10.1186/s13100-016-0070-z
Goodier JL, Zhang L, Vetter MR, Kazazian HH Jr (2007) LINE-1 ORF1 protein localizes in stress granules with other RNA-binding proteins, including components of RNA interference RNA-induced silencing complex. Mol Cell Biol 27:6469–6483. https://doi.org/10.1128/MCB.00332-07
Goodier JL, Cheung LE, Kazazian HH Jr (2012) MOV10 RNA helicase is a potent inhibitor of retrotransposition in cells. PLoS Genet 8:e1002941. https://doi.org/10.1371/journal.pgen.1002941
Goodier JL, Pereira GC, Cheung LE, Rose RJ, Kazazian HH Jr (2015) The broad-spectrum antiviral protein ZAP restricts human retrotransposition. PLoS Genet 11:e1005252. https://doi.org/10.1371/journal.pgen.1005252
Goodman RA, Macbeth MR, Beal PA (2012) ADAR proteins: structure and catalytic mechanism. Curr Top Microbiol Immunol 353:1–33. https://doi.org/10.1007/82_2011
Han JS, Szak ST, Boeke JD (2004) Transcriptional disruption by the L1 retrotransposon and implications for mammalian transcriptomes. Nature 429:268–274. https://doi.org/10.1038/nature02536
Hancks DC, Kazazian HH Jr (2016) Roles for retrotransposon insertions in human disease. Mob DNA 7:9. https://doi.org/10.1186/s13100-016-0065-9
Harris RS, Dudley JP (2015) APOBECs and virus restriction. Virology 479-480:131–145. https://doi.org/10.1016/j.virol.2015.03.012
Harris RS, Petersen-Mahrt SK, Neuberger MS (2002) RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators. Mol Cell 10:1247–1253
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (2003) DNA deamination mediates innate immunity to retroviral infection. Cell 113:803–809
Hartner JC, Walkley CR, Lu J, Orkin SH (2009) ADAR1 is essential for the maintenance of hematopoiesis and suppression of interferon signaling. Nat Immunol 10:109–115. https://doi.org/10.1038/ni.1680
Heras SR, Macias S, Cáceres JF, Garcia-Perez JL (2014) Control of mammalian retrotransposons by cellular RNA processing activities. Mob Genet Elem 4:e28439. https://doi.org/10.4161/mge.28439
Heraud-Farlow JE, Chalk AM, Linder SE, Li Q, Taylor S, White JM, Pang L, Liddicoat BJ, Gupte A, Li JB, Walkley CR (2017) Protein recoding by ADAR1-mediated RNA editing is not essential for normal development and homeostasis. Genome Biol 18:166. https://doi.org/10.1186/s13059-017-1301-4
Hogg M, Paro S, Keegan LP, O’Connell MA (2011) RNA editing by mammalian ADARs. Adv Genet 73:87–120. https://doi.org/10.1016/B978-0-12-380860-8.00003-3
Hohjoh H, Singer MF (1996) Cytoplasmic ribonucleoprotein complexes containing human LINE-1 protein and RNA. EMBO J 15:630–639
Holden LG, Prochnow C, Chang YP, Bransteitter R, Chelico L, Sen U, Stevens RC, Goodman MF, Chen XS (2008) Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications. Nature 456:121–124. https://doi.org/10.1038/nature07357
Holmes SE, Singer MF, Swergold GD (1992) Studies on p40, the leucine zipper motif-containing protein encoded by the first open reading frame of an active human LINE-1 transposable element. J Biol Chem 267:19765–19768
Honjo T, Muramatsu M, Fagarasan S (2004) AID: how does it aid antibody diversity? Immunity 20:659–668. https://doi.org/10.1016/j.immuni.2004.05.011
Horn AV, Klawitter S, Held U, Berger A, Vasudevan AA, Bock A, Hofmann H, Hanschmann KM, Trösemeier JH, Flory E, Jabulowsky RA, Han JS, Löwer J, Löwer R, Münk C, Schumann GG (2014) Human LINE-1 restriction by APOBEC3C is deaminase independent and mediated by an ORF1p interaction that affects LINE reverse transcriptase activity. Nucleic Acids Res 42:396–416. https://doi.org/10.1093/nar/gkt898
Hu S, Li J, Xu F, Mei S, Le Duff Y, Yin L, Pang X, Cen S, Jin Q, Liang C et al (2015) SAMHD1 inhibits LINE-1 Retrotransposition by promoting stress granule formation. PLoS Genet 11:e1005367. https://doi.org/10.1371/journal.pgen.1005367
Ikeda T, Abd El Galil KH, Tokunaga K, Maeda K, Sata T, Sakaguchi N, Heidmann T, Koito (2011) Intrinsic restriction activity by apolipoprotein B mRNA editing enzyme APOBEC1 against the mobility of autonomous retrotransposons. Nucleic Acids Res 39: 5538-4454. https://doi.org/10.1093/nar/gkr124
Ivanov A, Memczak S, Wyler E, Torti F, Porath HT, Orejuela MR, Piechotta M, Levanon EY, LandthalerM DC et al (2015) Analysis of intron sequences reveals hallmarks of circular RNA biogenesis in animals. Cell Rep 10:170–177. https://doi.org/10.1016/j.celrep.2014.12.019
Kaer K, Speek M (2013) Retroelements in human disease. Gene 518:231–241. https://doi.org/10.1016/j.gene.2013.01.008
Kazazian HH Jr, Moran JV (2017) Mobile DNA in health and disease. N Engl J Med 377:361–370. https://doi.org/10.1056/NEJMra1510092
Kazazian HH Jr, Wong C, Youssoufian H, Scott AF, Phillips DG, Antonarakis SE (1988) Haemophilia a resulting from de novo insertion of L1 sequences represents a novel mechanism for mutation in man. Nature 332:164–166. https://doi.org/10.1038/332164a0
Khan H, Smit A, Boissinot S (2006) Molecular evolution and tempo of amplification of human LINE-1 retrotransposons since the origin of primates. Genome Res 16:78–87. https://doi.org/10.1101/gr.40014
Khan MA, Goila-Gaur R, Opi S, Miyagi E, Takeuchi H, Kao S, Strebel K (2007) Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions. Retrovirology 4:48. https://doi.org/10.1186/1742-4690-4-48
Khazina E, Weichenrieder O (2009) Non-LTR retrotransposons encode noncanonical RRM domains in their first open reading frame. Proc Natl Acad Sci U S A 106:731–736. https://doi.org/10.1073/pnas.0809964106
Khazina E, Truffault V, Büttner R, Schmidt S, Coles M, Weichenrieder O (2011) Trimeric structure and flexibility of the L1ORF1 protein in human L1 retrotransposition. Nat Struct Mol Biol 18:1006–1114. https://doi.org/10.1038/nsmb.2097
Kinomoto M, Kanno T, Shimura M, Ishizaka Y, Kojima A, Kurata T, Sata T, Tokunaga K (2007) All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition. Nucleic Acids Res 35:2955–2964. https://doi.org/10.1093/nar/gkm181
Klawitter S, Fuchs NV, Upton KR, Muñoz-Lopez M, Shukla R et al (2016) Reprogramming triggers endogenous L1 and Alu retrotransposition in human induced pluripotent stem cells. Nat Commun 7:10286. https://doi.org/10.1038/ncomms10286
Knisbacher BA, Levanon EY (2015) DNA and RNA editing of retrotransposons accelerate mammalian genome evolution. Ann N Y Acad Sci 1341:115–125. https://doi.org/10.1111/nyas.12713
Knisbacher BA, Levanon EY (2016) DNA editing of LTR retrotransposons reveals the impact of APOBECs on vertebrate genomes. Mol Biol Evol 33:554–567. https://doi.org/10.1093/molbev/msv239
Koyama T, Arias JF, Iwabu Y, Yokoyama M, Fujita H, Sato H, Tokunaga K (2013) APOBEC3G oligomerization is associated with the inhibition of both Alu and LINE-1 retrotransposition. PLoS One 8:e84228. https://doi.org/10.1371/journal.pone.0084228
Kuramochi-Miyagawa S, Watanabe T, Gotoh K, Totoki Y, Toyoda A, Ikawa M et al (2008) DNA methylation of retrotransposon genes is regulated by Piwi family members MILI and MIWI2 in murine fetal testes. Genes Dev 22:908–917. https://doi.org/10.1101/gad.1640708
Lander ES, Linton LM, Birren B, Nusbaum C et al (2001) Initial sequencing and analysis of the human genome. Nature 409:860–921. https://doi.org/10.1038/35057062
LaRue RS, Andrésdóttir V, Blanchard Y, Conticello SG, Derse D, Emerman M, Greene WC, Jónsson SR, Landau NR, Löchelt M, Malik HS, Malim MH, Münk C, O’Brien SJ, Pathak VK, Strebel K, Wain-Hobson S, Yu XF, Yuhki N, Harris RS (2009) Guidelines for naming nonprimate APOBEC3 genes and proteins. J Virol 83:494–497. https://doi.org/10.1128/JVI.01976-08
Lecossier D, Bouchonnet F, Clavel F, Hance AJ (2003) Hypermutation of HIV-1 DNA in the absence of the Vif protein. Science 300:1112. https://doi.org/10.1126/science.1083338
Li Z, Woo CJ, Iglesias-Ussel MD, Ronai D, Scharff MD (2004) The generation of antibody diversity through somatic hypermutation and class switch recombination. Genes Dev 18:1–11. https://doi.org/10.1101/gad.1161904
Li Z, Okonski KM, Samuel CE (2012) Adenosine deaminase acting on RNA 1 (ADAR1) suppresses the induction of interferon by measles virus. J Virol 86:3787–3794. https://doi.org/10.1128/JVI.06307-11
Li P, Du J, Goodier JL, Hou J, Kang J, Kazazian HH Jr, Zhao K, Yu XF (2017) Aicardi-Goutières syndrome protein TREX1 suppresses L1 and maintains genome integrity through exonuclease-independent ORF1p depletion. Nucleic Acids Res 45:4619–4631. https://doi.org/10.1093/nar/gkx178
Liang W, Xu J, Yuan W, Song X, Zhang J, Wei W, Yu XF, Yang Y (2016) APOBEC3DE inhibits LINE-1 retrotransposition by interacting with ORF1p and influencing LINE reverse transcriptase activity. PLoS One 11:e0157220. https://doi.org/10.1371/journal.pone.0157220
Liddicoat BJ, Piskol R, Chalk AM, Ramaswami G, Higuchi M, Hartner JC, Li JB, Seeburg PH, Walkley CR (2015) RNA editing by ADAR1 prevents MDA5 sensing of endogenous dsRNA as nonself. Science 349:1115–11120. https://doi.org/10.1126/science.aac7049
Luan DD, Korman MH, Jakubczak JL, Eickbush TH (1993) Reverse transcription of R2Bm RNA is primed by a nick at the chromosomal target site: a mechanism for non-LTR retrotransposition. Cell 72:595–605
MacDuff DA, Demorest ZL, Harris RS (2009) AID can restrict L1 retrotransposition suggesting a dual role in innate and adaptive immunity. Nucleic Acids Res 37:1854–1867. https://doi.org/10.1093/nar/gkp030
Macia A, Widmann TJ, Heras SR, Ayllon V, Sanchez L, Benkaddour-Boumzaouad M, Muñoz-Lopez M, Rubio A, Amador-Cubero S, Blanco-Jimenez E, Garcia-Castro J, Menendez P, Ng P, Muotri AR, Goodier JL, Garcia-Perez JL (2017) Engineered LINE-1 retrotransposition in nondividing human neurons. Genome Res 27:335–348. https://doi.org/10.1101/gr.206805
Mager DL, Stoye JP (2015) Mammalian endogenous retroviruses. Microbiol Spectrom 3:MDNA3-0009-2014. https://doi.org/10.1128/microbiolspec.MDNA3-0009-2014
Malone CD, Brennecke J, Dus M, Stark A, McCombie WR, Sachidanandam R, Hannon GJ (2009) Specialized piRNA pathways act in germline and somatic tissues of the drosophila ovary. Cell 137:522–535. https://doi.org/10.1016/j.cell.2009.03.040
Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D (2003) Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424:99–103. https://doi.org/10.1038/nature01709
Mannion NM, Greenwood SM, Young R, Cox S, Brindle J, Read D, Nellaker C, Vesely C, Ponting CP, McLaughlin PJ et al (2014) The RNA editing enzyme ADAR1 controls innate immune responses to RNA. Cell Rep 9:1482–1494. https://doi.org/10.1016/j.celrep.2014.10.041
Mannion N, Arieti F, Gallo A, Keegan LP, O’Connell MA (2015) New insights into the biological role of mammalian ADARs: the RNA editing proteins. Biomol Ther 5:2338–2362. https://doi.org/10.3390/biom5042338
Marino D, Perković M, Hain A, Jaguva Vasudevan AA, Hofmann H, Hanschmann KM, Mühlebach MD, Schumann GG, König R, Cichutek K, Häussinger D (2016) Münk C (2016) APOBEC4 enhances the replication of HIV-1. PLoS One 11:e0155422. https://doi.org/10.1371/journal.pone.0155422
Martens JH, O’Sullivan RJ, Braunschweig U, Opravil S, Radolf M, Steinlein P, Jenuwein T (2005) The profile of repeat-associated histone lysine methylation states in the mouse epigenome. EMBO J 24:800–812. https://doi.org/10.1038/sj.emboj.7600545
Martin SL (2010) Nucleic acid chaperone properties of ORF1p from the non-LTR retrotransposon, LINE-1. RNA Biol 7:706–711
Martin SL, Bushman FD (2001) Nucleic acid chaperone activity of the ORF1 protein from the mouse LINE-1 retrotransposon. Mol Cell Biol 21:467–475
Mathias SL, Scott AF, Kazazian HH Jr, Boeke JD, Gabriel A (1991) Reverse transcriptase encoded by a human transposable element. Science 254:1808–1810
McDougall WM, Smith HC (2011) Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity. Biochem Biophys Res Commun 412:612–617. https://doi.org/10.1016/j.bbrc.2011.08.009
Melcher T, Maas S, Higuchi M, Keller W, Seeburg PH (1995) Editing of AMPA receptor GluR-B pre-mRNA in vitro reveals site-selective adenosine to inosine conversion. J Biol Chem 270:8566–8570. https://doi.org/10.1074/jbc.270.15.8566
Miyamura Y, Suzuki T, Kono M, Inagaki K, Ito S, Suzuki N, Tomita Y (2003) Mutations of the RNA-specific adenosine deaminase gene (DSRAD) are involved in dyschromatosis symmetrica hereditaria. Am J Hum Genet 73:693–699
Moldovan JB, Moran JV (2015) The zinc-finger antiviral protein ZAP inhibits LINE and Alu retrotransposition. PLoS Genet 11:e1005121. https://doi.org/10.1371/journal.pgen.1005121
Muckenfuss H, Hamdorf M, Held U, Perkovic M, Lower J, Cichutek K et al (2006) APOBEC3 proteins inhibit human LINE-1 retrotransposition. J Biol Chem 281:22161–22172. https://doi.org/10.1074/jbc.M601716200
Muotri AR, Chu VT, Marchetto MC, Deng W, Moran JV, Gage FH (2005) Somatic mosaicism in neuronal precursor cells mediated by L1 retrotransposition. Nature 435:903–910. https://doi.org/10.1038/nature03663
Muotri AR, Marchetto MC, Coufal NG, Oefner R, Yeo G, Nakashima K, Gage FH (2010) L1 retrotransposition in neurons is modulated by MeCP2. Nature 468:443–446. https://doi.org/10.1038/nature09544
Muramatsu M, Sankaranand VS, Anant S, Sugai M, Kinoshita K, Davidson NO, Honjo T (1999) Specific expression of activation-induced cytidine deaminase (AID), a novel member of the RNA-editing deaminase family in germinal center B cells. J Biol Chem 274:18470–18476
Navaratnam N, Bhattacharya S, Fujino T, Patel D, Jarmuz AL, Scott J (1995) Evolutionary origins of apoB mRNA editing: catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site. Cell 81:187–195
Niewiadomska AM, Tian C, Tan WT, Sarkis PT, Yu XF (2007) Differential inhibition of long interspersed element 1 by APOBEC3 does not correlate with high-molecular-mass-complex formation or P-body association. J Virol 81:9577–9583. https://doi.org/10.1128/JVI.02800-06
Nishikura K (2016) A-to-I editing of coding and non-coding RNAs by ADARs. Nat Rev Mol Cell Biol 17:83–96. https://doi.org/10.1038/nrm.2015.4
Orecchini E, Federico M, Doria M, Arenaccio C, Giuliani E, Ciafrè SA, Michienzi A (2015) The ADAR1 editing enzyme is encapsidated into HIV-1 virions. Virology 485:475–480. https://doi.org/10.1016/j.virol.2015.07.027
Orecchini E, Doria M, Antonioni A, Galardi S, Ciafrè SA, Frassinelli L, Mancone C, Montaldo C, Tripodi M, Michienzi A (2017a) ADAR1 restricts LINE-1 retrotransposition. Nucleic Acids Res 45:155–168. https://doi.org/10.1093/nar/gkw834
Orecchini E, Frassinelli L, Michienzi A (2017b) Restricting retrotransposons: ADAR1 is another guardian of the human genome. RNA Biol 22:1–7. https://doi.org/10.1080/15476286.2017.1341033
Orgel LE, Crick FH, Sapienza (1980) Selfish DNA. Nature 288:645–646
Ostertag EM, Goodier JL, Zhang Y, Kazazian HH Jr (2003) SVA elements are nonautonomous retrotransposons that cause disease in humans. Am J Hum Genet 73:1444–1451. https://doi.org/10.1086/380207
Pace JK 2nd, Feschotte C (2007) The evolutionary history of human DNA transposons: evidence for intense activity in the primate lineage. Genome Res 17:422–432. https://doi.org/10.1101/gr.5826307
Papavasiliou FN, Schatz DG (2002) Somatic hypermutation of immunoglobulin genes: merging mechanisms for genetic diversity. Cell 109(Suppl):S35–S44
Patterson JB, Samuel CE (1995) Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase. Mol Cell Biol 15:5376–5388
Perepelitsa-Belancio V, Deininger P (2003) RNA truncation by premature polyadenylation attenuates human mobile element activity. Nat Genet 35:363–366. https://doi.org/10.1038/ng1269
Pestal K, Funk CC, Snyder JM, Price ND, Treuting PM, Stetson DB (2015) Isoforms of RNA-editing enzyme ADAR1 independently control nucleic acid sensor MDA5-driven autoimmunity and multi-organ development. Immunity 43:933–494. https://doi.org/10.1016/j.immuni.2015.11.001
Petersen-Mahrt SK, Neuberger MS (2003) In vitro deamination of cytosine to uracil in single-stranded DNA by apolipoprotein B editing complex catalytic subunit 1 (APOBEC1). J Biol Chem 278:19583–19586. https://doi.org/10.1074/jbc.C300114200
Petersen-Mahrt SK, Harris RS, Neuberger MS (2002) AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification. Nature 418:99–103. https://doi.org/10.1038/nature00862
Piskareva O, Ernst C, Higgins N, Schmatchenko V (2013) The carboxy-terminal segment of the human LINE-1 ORF2 protein is involved in RNA binding. FEBS Open Bio 3:433–437. https://doi.org/10.1016/j.fob.2013.09.005
Pizarro JG, Cristofari G (2016) Post-transcriptional control of LINE-1 retrotransposition by cellular host factors in somatic cells. Front Cell Dev Biol 4:14. https://doi.org/10.3389/fcell.2016.00014
Prasanth KV, Prasanth SG, Xuan Z, Hearn S, Freier SM, Bennett CF, Zhang MQ, Spector DL (2005) Regulating gene expression through RNA nuclear retention. Cell 123:249–263. https://doi.org/10.1016/j.cell.2005.08.033
Prohaska KM, Bennett RP, Salter JD, Smith HC (2014) The multifaceted roles of RNA binding in APOBEC cytidine deaminase functions. Wiley Interdiscip Rev RNA 5:493–508. https://doi.org/10.1002/wrna.1226
Raiz J, Damert A, Chira S, Held U, Klawitter S, Hamdorf M, Löwer J, Strätling WH, Löwer R, Schumann GG (2012) The non-autonomous retrotransposon SVA is trans-mobilized by the human LINE-1 protein machinery. Nucleic Acids Res 40:1666–1683. https://doi.org/10.1093/nar/gkr863
Ramaswami G, Lin W, Piskol R, Tan MH, Davis C, Li JB (2012) Accurate identification of human Alu and non-Alu RNA editing sites. Nat Methods 9:579–581. https://doi.org/10.1038/nmeth.1982
Rayon-Estrada V, Papavasiliou FN, Harjanto D (2015) RNA editing dynamically rewrites the cancer code. Trends Cancer 1:211–212. https://doi.org/10.1016/j.trecan.2015.10.008
Rayon-Estrada V, Harjanto D, Hamilton CE, Berchiche YA, Gantman EC, Sakmar TP, Bulloch K, Gagnidze K, Harroch S, McEwen BS, Papavasiliou FN (2017) Epitranscriptomic profiling across cell types reveals associations between APOBEC1-mediated RNA editing, gene expression outcomes, and cellular function. Proc Natl Acad Sci U S A 114:13296–13301. https://doi.org/10.1073/pnas.1714227114
Rebagliati MR, Melton DA (1987) Antisense RNA injections in fertilized frog eggs reveal an RNA duplex unwinding activity. Cell 48:599–605
Refsland EW, Stenglein MD, Shindo K, Albin JS, Brown WL, Harris RS (2010) Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes and tissues: implications for HIV-1 restriction. Nucleic Acids Res 38:4274–4284. https://doi.org/10.1093/nar/gkq174
Rice GI, Kasher PR, Forte GM, Mannion NM, Greenwood SM, Szynkiewicz M et al (2012) Mutations in ADAR1 cause Aicardi-Goutières syndrome associated with a type I interferon signature. Nat Genet 44:1243–1248. https://doi.org/10.1038/ng.2414
Richardson SR, Narvaiza I, Planegger RA, Weitzman MD, Moran JV (2014) APOBEC3A deaminates transiently exposed single-strand DNA during LINE-1 retrotransposition. elife 3:e02008. https://doi.org/10.7554/eLife.02008
Richardson SR, Doucet AJ, Kopera HC, Moldovan JB, Garcia-Perez JL, Moran JV (2015) The influence of LINE-1 and SINE retrotransposons on mammalian genomes. Microbiol Spectrom 3:MDNA3-0061-2014. https://doi.org/10.1128/microbiolspec.MDNA3-0061-2014
Richardson SR, Gerdes P, Gerhardt DJ, Sanchez-Luque FJ, Bodea GO, Muñoz-Lopez M, Jesuadian JS, Kempen MHC, Carreira PE, Jeddeloh JA, Garcia-Perez JL, Kazazian HH Jr, Ewing AD, Faulkner GJ (2017) Heritable L1 retrotransposition in the mouse primordial germline and early embryo. Genome Res 27:1395–1405. https://doi.org/10.1101/gr.219022.116
Riedmann EM, Schopoff S, Hartner JC, Jantsch MF (2008) Specificity of ADAR-mediated RNA editing in newly identified targets. RNA 14:1110–1118. https://doi.org/10.1261/rna.923308
Rosenberg BR, Hamilton CE, Mwangi MM, Dewell S, Papavasiliou FN (2012) Transcriptome-wide sequencing reveals numerous APOBEC1 mRNA-editing targets in transcript 3' UTRs. Nat Struct Mol Biol 18: 230-236. https://doi.org/10.1038/nsmb.1975.
Rueter SM, Dawson TR, Emeson RB (1999) Regulation of alternative splicing by RNA editing. Nature 399:75–80. https://doi.org/10.1038/19992
Russell SJ, Stalker L, LaMarre J (2017) PIWIs, piRNAs and retrotransposons: complex battles during reprogramming in gametes and early embryos. Reprod Domest Anim 52(Suppl 4):28–38. https://doi.org/10.1111/rda.13053
Salter JD, Bennett RP, Smith HC (2016) The APOBEC protein family: united by structure, divergent in function. Trends Biochem Sci 41:578–594. https://doi.org/10.1016/j.tibs.2016.05.001
Samuel CE (2011) Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral. Virology 411:180–193. https://doi.org/10.1016/j.virol.2010.12.004
Sassaman DM, Dombroski BA, Moran JV, Kimberland ML, Naas TP, DeBerardinis RJ, Gabriel A, Swergold GD, Kazazian HH Jr (1997) Many human L1 elements are capable of retrotransposition. Nat Genet 16:37–43. https://doi.org/10.1038/ng0597-37
Scarfò I, Pellegrino E, Mereu E, Inghirami G, Piva R (2016) Transposable elements: the enemies within. Exp Hematol 44:913–916. https://doi.org/10.1016/j.exphem.2016.06.251
Schumann GG (2007) APOBEC3 proteins: major players in intracellular defence against LINE-1-mediated retrotransposition. Biochem Soc Trans 35:637–642. https://doi.org/10.1042/BST0350637
Sharma S, Patnaik SK, Taggart RT, Kannisto ED, Enriquez SM, Gollnick P, Baysal BE (2015) APOBEC3A cytidine deaminase induces RNA editing in monocytes and macrophages. Nat Commun 6:6881. https://doi.org/10.1038/ncomms7881
Sheehy AM, Gaddis NC, Choi JD, Malim MH (2002) Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646–650. https://doi.org/10.1038/nature00939
Sheinberger J, Shav-Tal Y (2017) mRNPs meet stress granules. FEBS Lett 591:2534–2542. https://doi.org/10.1002/1873-3468.12765
Siriwardena SU, Chen K, Bhagwat AS (2016) Functions and malfunctions of mammalian DNA-cytosine deaminases. Chem Rev 116:12688–12710. https://doi.org/10.1021/acs.chemrev.6b00296
Smith HC (2016) RNA binding to APOBEC deaminases; not simply a substrate for C to U editing. RNA Biol 21:1–13. https://doi.org/10.1080/15476286.2016.1259783
Sohail A, Klapacz J, Samaranayake M, Ullah A, Bhagwat AS (2003) Human activation-induced cytidine deaminase causes transcription-dependent, strand-biased C to U deaminations. Nucleic Acids Res 31:2990–2994
Song C, Sakurai M, Shiromoto Y, Nishikura K (2016) Functions of the RNA editing enzyme ADAR1 and their relevance to human diseases. Genes (Basel) 7:E129. https://doi.org/10.3390/genes7120129
Speek M (2001) Antisense promoter of human L1 retrotransposon drives transcription of adjacent cellular genes. Mol Cell Biol 21:1973–1985. https://doi.org/10.1128/MCB.21.6.1973-1985.2001
Stenglein MD, Harris RS (2006) APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism. J Biol Chem 281(16837):16841. https://doi.org/10.1074/jbc.M602367200
Stetson DB, Ko JS, Heidmann T, Medzhitov R (2008) Trex1 prevents cell-intrinsic initiation of autoimmunity. Cell 134:587–598. https://doi.org/10.1016/j.cell.2008.06.032
Stocking C, Kozak CA (2008) Murine endogenous retroviruses. Cell Mol Life Sci 65:3383–3398. https://doi.org/10.1007/s00018-008-8497-0
Stoye JP (2012) Studies of endogenous retroviruses reveal a continuino evolutionary saga. Nat Rev Microbiol 10:395–406. https://doi.org/10.1038/nrmicro2783
Strehblow A, Hallegger M, Jantsch MF (2002) Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-rich export signal, and a putative dimerization domain. Mol Biol Cell 13:3822–3835. https://doi.org/10.1091/mbc.E02-03-0161
Swanton C, McGranahan N, Starrett GJ, Harris RS (2015) APOBEC enzymes: mutagenic fuel for cancer evolution and heterogeneity. Cancer Discov 5:704–712. https://doi.org/10.1158/2159-8290.CD-15-0344
Tan L, Sarkis PT, Wang T, Tian C, Yu XF (2009) Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1. FASEB J 23:279–287. https://doi.org/10.1096/fj.07-088781
Teng B, Burant CF, Davidson NO (1993) Molecular cloning of an apolipoprotein B messenger RNA editing protein. Science 260:1816–1819
Tomaselli S, Galeano F, Locatelli F, Gallo A (2015) ADARs and the balance game between virus infection and innate immune cell response. Curr Issues Mol Biol 17:37–51
van den Hurk JA, Meij IC, Seleme MC, Kano H, Nikopoulos K, Hoefsloot LH, Sistermans EA, de Wijs IJ, Mukhopadhyay A, Plomp AS, de Jong PT, Kazazian HH, Cremers FP (2007) L1 retrotransposition can occur early in human embryonic development. Hum Mol Genet 16:1587–1592. https://doi.org/10.1093/hmg/ddm108
Vesely C, Tauber S, Sedlazeck FJ, von Haeseler A, Jantsch MF (2012) Adenosine deaminases that act on RNA induce reproducible changes in abundance and sequence of embryonic miRNAs. Genome Res 22:1468–1476. https://doi.org/10.1101/gr.133025.111
Vesely C, Tauber S, Sedlazeck FJ, Tajaddod M, von Haeseler A, Jantsch MF (2014) ADAR2 induces reproducible changes in sequence and abundance of mature microRNAs in the mouse brain. Nucleic Acids Res 42:12155–12168. https://doi.org/10.1093/nar/gks590
Wang IX, So E, Devlin JL, Zhao Y, Wu M, Cheung VG (2013) ADAR regulates RNA editing, transcript stability, and gene expression. Cell Rep 5:849–860. https://doi.org/10.1016/j.celrep.2013.10.002
Weissbach R, Scadden AD (2012) Tudor-SN and ADAR1 are components of cytoplasmic stress granules. RNA 18:462–471. https://doi.org/10.1261/rna.027656.111
Wichroski MJ, Robb GB, Rana TM (2006) Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies. PLoS Pathog 2:e41. https://doi.org/10.1371/journal.ppat.0020041
Wissing S, Montano M, Garcia-Perez JL, Moran JV, Greene WC (2011) Endogenous APOBEC3B restricts LINE-1 retrotransposition in transformed cells and human embryonic stem cells. J Biol Chem 286:36427–36437. https://doi.org/10.1074/jbc.M111.251058
Wissing S, Munoz-Lopez M, Macia A, Yang Z, Montano M, Collins W, Garcia-Perez JL, Moran JV, Greene WC (2012) Reprogramming somatic cells into iPS cells activates LINE-1 retroelement mobility. Hum Mol Genet 21:208–218. https://doi.org/10.1093/hmg/ddr455
Yoder JA, Walsh CP, Bestor TH (1997) Cytosine methylation and the ecology of intragenomic parasites. Trends Genet 13:335–340
Zamudio N, Bourc’his D (2010) Transposable elements in the mammalian germline: a comfortable niche or a deadly trap? Heredity 105:92–104. https://doi.org/10.1038/hdy.2010.53
Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424:94–98. https://doi.org/10.1038/nature01707
Zhang A, Dong B, Doucet AJ, Moldovan JB, Moran JV, Silverman RH (2014) RNase L restricts the mobility of engineered retrotransposons in cultured human cells. Nucleic Acids Res 42:3803–3820. https://doi.org/10.1093/nar/gkt1308
Zhang P, Ludwig AK, Hastert FD, Rausch C, Lehmkuhl A, Hellmann I, Smets M, Leonhardt H, Cardoso MC (2017) L1 retrotransposition is activated by ten-eleven-translocation protein 1 and repressed by methyl-CpG binding proteins. Nucleus 8:548–562. https://doi.org/10.1080/19491034.2017.1330238
Zhao K, Du J, Han X, Goodier JL, Li P, Zhou X, Wei W, Evans SL, Li L, Zhang W, Cheung LE, Wang G, Kazazian HH Jr, Yu XF (2013) Modulation of LINE-1 and Alu/SVA retrotransposition by Aicardi-Goutières syndrome-related SAMHD1. Cell Rep 4:1108–1115. https://doi.org/10.1016/j.celrep.2013.08.019
Zheng S, Vuong BQ, Vaidyanathan B, Lin JY, Huang FT, Chaudhuri J (2015) Non-coding RNA generated following lariat debranching mediates targeting of AID to DNA. Cell 161:762–773. https://doi.org/10.1016/j.cell.2015.03.020
Zheng Y, Lorenzo C, Beal PA (2017) DNA editing in DNA/RNA hybrids by adenosine deaminases that act on RNA. Nucleic Acids Res 45:3369–3377. https://doi.org/10.1093/nar/gkx050
Acknowledgements
The authors would like to thank Dr. Silvo Conticello for critical reading of the manuscript.
This study was supported in part by Telethon-Italy [GGP15227 to A.M.].
Author information
Authors and Affiliations
Corresponding author
Additional information
Responsible Editor: Peter A. Larsen
Rights and permissions
About this article
Cite this article
Orecchini, E., Frassinelli, L., Galardi, S. et al. Post-transcriptional regulation of LINE-1 retrotransposition by AID/APOBEC and ADAR deaminases. Chromosome Res 26, 45–59 (2018). https://doi.org/10.1007/s10577-018-9572-5
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10577-018-9572-5