Ribonucleases pp 223-244 | Cite as

The RNA Exosomes

  • Karl-Peter HopfnerEmail author
  • Sophia Hartung
Part of the Nucleic Acids and Molecular Biology book series (NUCLEIC)


RNA exosomes are large multimeric 3′-5′ exo- and endonucleases found in eukaryotes and many archaeal species. They represent the central RNA 3′-end processing factor and are implicated in processing, quality control, and turnover of both coding and noncoding RNAs. RNA exosomes are highly regulated and processive machineries, assembled as large macromolecular cages that channel RNA to the ribonuclease sites. The primordial exosome – found in archaea and related to bacterial and organelle degradosomes – possesses a phosphorolytic active cage that can both degrade and polyadenylate RNA in RNA decay processes. Human and yeast exosomes lost phosphorolytic activities but gained ectopic subunits with hydrolytic activities, while preserving the RNA channeling function.


Processing Chamber Exosome Complex Transcription Elongation Complex Exit Pore Phosphorolytic Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



Work in KPHs laboratory on exosomes is supported by a grant from the German Research Council (DFG HO2489/3).


  1. Allmang C, Kufel J, Chanfreau G, Mitchell P, Petfalski E, Tollervey D (1999a) Functions of the exosome in rRNA, snoRNA and snRNA synthesis. EMBO J 18:5399–5410PubMedGoogle Scholar
  2. Allmang C, Petfalski E, Podtelejnikov A, Mann M, Tollervey D, Mitchell P (1999b) The yeast exosome and human PM-Scl are related complexes of 3′ –> 5′ exonucleases. Genes Dev 13:2148–2158PubMedGoogle Scholar
  3. Allmang C, Mitchell P, Petfalski E, Tollervey D (2000) Degradation of ribosomal RNA precursors by the exosome. Nucleic Acids Res 28:1684–1691PubMedGoogle Scholar
  4. Anderson JS, Parker RP (1998) The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex. EMBO J 17:1497–1506PubMedGoogle Scholar
  5. Andrulis ED, Werner J, Nazarian A, Erdjument-Bromage H, Tempst P, Lis JT (2002) The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila. Nature 420:837–841PubMedGoogle Scholar
  6. Araki Y, Takahashi S, Kobayashi T, Kajiho H, Hoshino S, Katada T (2001) Ski7p G protein interacts with the exosome and the Ski complex for 3′-to-5′ mRNA decay in yeast. EMBO J 20:4684–4693PubMedGoogle Scholar
  7. Basu U, Meng FL, Keim C, Grinstein V, Pefanis E, Eccleston J, Zhang T, Myers D, Wasserman CR, Wesemann DR et al (2011) The RNA exosome targets the AID cytidine deaminase to both strands of transcribed duplex DNA substrates. Cell 144:353–363PubMedGoogle Scholar
  8. Belgrader P, Cheng J, Zhou X, Stephenson LS, Maquat LE (1994) Mammalian nonsense codons can be cis effectors of nuclear mRNA half-life. Mol Cell Biol 14:8219–8228PubMedGoogle Scholar
  9. Bernstein J, Patterson DN, Wilson GM, Toth EA (2008) Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3′-> 5′ helicase partner of the nuclear exosome. J Biol Chem 283:4930–4942PubMedGoogle Scholar
  10. Bonneau F, Basquin J, Ebert J, Lorentzen E, Conti E (2009) The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation. Cell 139:547–559PubMedGoogle Scholar
  11. Bousquet-Antonelli C, Presutti C, Tollervey D (2000) Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102:765–775PubMedGoogle Scholar
  12. Buttner K, Wenig K, Hopfner KP (2005) Structural framework for the mechanism of archaeal exosomes in RNA processing. Mol Cell 20:461–471PubMedGoogle Scholar
  13. Buttner K, Nehring S, Hopfner KP (2007) Structural basis for DNA duplex separation by a superfamily-2 helicase. Nat Struct Mol Biol 14:647–652PubMedGoogle Scholar
  14. Callahan KP, Butler JS (2010) TRAMP complex enhances RNA degradation by the nuclear exosome component Rrp6. J Biol Chem 285:3540–3547PubMedGoogle Scholar
  15. Camblong J, Iglesias N, Fickentscher C, Dieppois G, Stutz F (2007) Antisense RNA stabilization induces transcriptional gene silencing via histone deacetylation in S. cerevisiae. Cell 131:706–717PubMedGoogle Scholar
  16. Carninci P (2010) RNA dust: where are the genes? DNA Res 17:51–59PubMedGoogle Scholar
  17. Chekanova JA, Shaw RJ, Wills MA, Belostotsky DA (2000) Poly(A) tail-dependent exonuclease AtRrp41p from Arabidopsis thaliana rescues 5.8 S rRNA processing and mRNA decay defects of the yeast ski6 mutant and is found in an exosome-sized complex in plant and yeast cells. J Biol Chem 275:33158–33166PubMedGoogle Scholar
  18. Chekanova JA, Gregory BD, Reverdatto SV, Chen H, Kumar R, Hooker T, Yazaki J, Li P, Skiba N, Peng Q et al (2007) Genome-wide high-resolution mapping of exosome substrates reveals hidden features in the Arabidopsis transcriptome. Cell 131:1340–1353PubMedGoogle Scholar
  19. Chen CY, Gherzi R, Ong SE, Chan EL, Raijmakers R, Pruijn GJ, Stoecklin G, Moroni C, Mann M, Karin M (2001) AU binding proteins recruit the exosome to degrade ARE-containing mRNAs. Cell 107:451–464PubMedGoogle Scholar
  20. Cheng Z, Liu Y, Wang C, Parker R, Song H (2004) Crystal structure of Ski8p, a WD-repeat protein with dual roles in mRNA metabolism and meiotic recombination. Protein Sci 13:2673–2684PubMedGoogle Scholar
  21. Cristodero M, Clayton CE (2007) Trypanosome MTR4 is involved in rRNA processing. Nucleic Acids Res 35:7023–7030PubMedGoogle Scholar
  22. Cristodero M, Bottcher B, Diepholz M, Scheffzek K, Clayton C (2008) The Leishmania tarentolae exosome: purification and structural analysis by electron microscopy. Mol Biochem Parasitol 159:24–29PubMedGoogle Scholar
  23. de la Cruz J, Kressler D, Tollervey D, Linder P (1998) Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3′ end formation of 5.8 S rRNA in Saccharomyces cerevisiae. EMBO J 17:1128–1140PubMedGoogle Scholar
  24. Deutscher MP, Reuven NB (1991) Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis. Proc Natl Acad Sci USA 88:3277–3280PubMedGoogle Scholar
  25. Dziembowski A, Lorentzen E, Conti E, Seraphin B (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14:15–22PubMedGoogle Scholar
  26. Estevez AM, Kempf T, Clayton C (2001) The exosome of Trypanosoma brucei. EMBO J 20:3831–3839PubMedGoogle Scholar
  27. Evguenieva-Hackenberg E, Walter P, Hochleitner E, Lottspeich F, Klug G (2003) An exosome-like complex in Sulfolobus solfataricus. EMBO Rep 4:889–893PubMedGoogle Scholar
  28. Evguenieva-Hackenberg E, Roppelt V, Finsterseifer P, Klug G (2008) Rrp4 and Csl4 are needed for efficient degradation but not for polyadenylation of synthetic and natural RNA by the archaeal exosome. Biochemistry 47:13158–13168PubMedGoogle Scholar
  29. Evguenieva-Hackenberg E, Roppelt V, Lassek C, Klug G (2011) Subcellular localization of RNA degrading proteins and protein complexes in prokaryotes. RNA Biol 8:49–54Google Scholar
  30. Fang F, Phillips S, Butler JS (2005) Rat1p and Rai1p function with the nuclear exosome in the processing and degradation of rRNA precursors. RNA 11:1571–1578PubMedGoogle Scholar
  31. Frischmeyer PA, van Hoof A, O'Donnell K, Guerrerio AL, Parker R, Dietz HC (2002) An mRNA surveillance mechanism that eliminates transcripts lacking termination codons. Science 295:2258–2261PubMedGoogle Scholar
  32. Goodchild A, Raftery M, Saunders NF, Guilhaus M, Cavicchioli R (2004) Biology of the cold adapted archaeon, Methanococcoides burtonii determined by proteomics using liquid chromatography-tandem mass spectrometry. J Proteome Res 3:1164–1176PubMedGoogle Scholar
  33. Grosshans H, Deinert K, Hurt E, Simos G (2001) Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export. J Cell Biol 153:745–762PubMedGoogle Scholar
  34. Guo J, Cheng P, Yuan H, Liu Y (2009) The exosome regulates circadian gene expression in a posttranscriptional negative feedback loop. Cell 138:1236–1246PubMedGoogle Scholar
  35. Haile S, Estevez AM, Clayton C (2003) A role for the exosome in the in vivo degradation of unstable mRNAs. RNA 9:1491–1501PubMedGoogle Scholar
  36. Harlow LS, Kadziola A, Jensen KF, Larsen S (2004) Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding. Protein Sci 13:668–677PubMedGoogle Scholar
  37. Hartung S, Hopfner KP (2009) Lessons from structural and biochemical studies on the archaeal exosome. Biochem Soc Trans 37:83–87PubMedGoogle Scholar
  38. Hartung S, Niederberger T, Hartung M, Tresch A, Hopfner KP (2010) Quantitative analysis of processive RNA degradation by the archaeal RNA exosome. Nucleic Acids Res 38:5166–5176PubMedGoogle Scholar
  39. Hilleren PJ, Parker R (2003) Cytoplasmic degradation of splice-defective pre-mRNAs and intermediates. Mol Cell 12:1453–1465PubMedGoogle Scholar
  40. Hilleren P, McCarthy T, Rosbash M, Parker R, Jensen TH (2001) Quality control of mRNA 3′-end processing is linked to the nuclear exosome. Nature 413:538–542PubMedGoogle Scholar
  41. Houseley J, Tollervey D (2006) Yeast Trf5p is a nuclear poly(A) polymerase. EMBO Rep 7:205–211PubMedGoogle Scholar
  42. Iyer LM, Koonin EV, Leipe DD, Aravind L (2005) Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members. Nucleic Acids Res 33:3875–3896PubMedGoogle Scholar
  43. Jackson RN, Klauer AA, Hintze BJ, Robinson H, van Hoof A, Johnson SJ (2010) The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. EMBO J 29:2205–2216PubMedGoogle Scholar
  44. Kadaba S, Krueger A, Trice T, Krecic AM, Hinnebusch AG, Anderson J (2004) Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae. Genes Dev 18:1227–1240PubMedGoogle Scholar
  45. Kawamoto H, Morita T, Shimizu A, Inada T, Aiba H (2005) Implication of membrane localization of target mRNA in the action of a small RNA: mechanism of post-transcriptional regulation of glucose transporter in Escherichia coli. Genes Dev 19:328–338PubMedGoogle Scholar
  46. Khemici V, Poljak L, Luisi BF, Carpousis AJ (2008) The RNase E of Escherichia coli is a membrane-binding protein. Mol Microbiol 70:799–813PubMedGoogle Scholar
  47. Koonin EV, Wolf YI, Aravind L (2001) Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach. Genome Res 11:240–252PubMedGoogle Scholar
  48. LaCava J, Houseley J, Saveanu C, Petfalski E, Thompson E, Jacquier A, Tollervey D (2005) RNA degradation by the exosome is promoted by a nuclear polyadenylation complex. Cell 121:713–724PubMedGoogle Scholar
  49. Lebreton A, Tomecki R, Dziembowski A, Seraphin B (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456:993–996PubMedGoogle Scholar
  50. Lee G, Hartung S, Hopfner KP, Ha T (2010) Reversible and Controllable Nanolocomotion of an RNA-Processing Machinery. Nano LettGoogle Scholar
  51. Lejeune F, Li X, Maquat LE (2003) Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol Cell 12:675–687PubMedGoogle Scholar
  52. Liu Q, Greimann JC, Lima CD (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127:1223–1237PubMedGoogle Scholar
  53. Lorentzen E, Conti E (2005) Structural basis of 3′ end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core. Mol Cell 20:473–481PubMedGoogle Scholar
  54. Lorentzen E, Walter P, Fribourg S, Evguenieva-Hackenberg E, Klug G, Conti E (2005) The archaeal exosome core is a hexameric ring structure with three catalytic subunits. Nat Struct Mol Biol 12:575–581PubMedGoogle Scholar
  55. Lorentzen E, Dziembowski A, Lindner D, Seraphin B, Conti E (2007) RNA channelling by the archaeal exosome. EMBO Rep 8:470–476PubMedGoogle Scholar
  56. Lorentzen E, Basquin J, Tomecki R, Dziembowski A, Conti E (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29:717–728PubMedGoogle Scholar
  57. Lu C, Ding F, Ke A (2010) Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring. PLoS ONE 5:e8739PubMedGoogle Scholar
  58. Luz JS, Ramos CR, Santos MC, Coltri PP, Palhano FL, Foguel D, Zanchin NI, Oliveira CC (2010) Identification of archaeal proteins that affect the exosome function in vitro. BMC Biochem 11:22PubMedGoogle Scholar
  59. Madrona AY, Wilson DK (2004) The structure of Ski8p, a protein regulating mRNA degradation: implications for WD protein structure. Protein Sci 13:1557–1565PubMedGoogle Scholar
  60. Malet H, Topf M, Clare DK, Ebert J, Bonneau F, Basquin J, Drazkowska K, Tomecki R, Dziembowski A, Conti E et al (2010) RNA channelling by the eukaryotic exosome. EMBO Rep 11:936–942PubMedGoogle Scholar
  61. Maniatis T, Reed R (2002) An extensive network of coupling among gene expression machines. Nature 416:499–506PubMedGoogle Scholar
  62. Midtgaard SF, Assenholt J, Jonstrup AT, Van LB, Jensen TH, Brodersen DE (2006) Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain. Proc Natl Acad Sci USA 103:11898–11903PubMedGoogle Scholar
  63. Mitchell P, Tollervey D (2003) An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3′– > 5′ degradation. Mol Cell 11:1405–1413PubMedGoogle Scholar
  64. Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D (1997) The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′– > 5′ exoribonucleases. Cell 91:457–466PubMedGoogle Scholar
  65. Mohanty BK, Kushner SR (2000) Polynucleotide phosphorylase, RNase II and RNase E play different roles in the in vivo modulation of polyadenylation in Escherichia coli. Mol Microbiol 36:982–994PubMedGoogle Scholar
  66. Navarro MV, Oliveira CC, Zanchin NI, Guimaraes BG (2008) Insights into the mechanism of progressive RNA degradation by the archaeal exosome. J Biol Chem 283:14120–14131PubMedGoogle Scholar
  67. Nevo-Dinur K, Nussbaum-Shochat A, Ben-Yehuda S, Amster-Choder O (2011) Translation-independent localization of mRNA in E. coli. Science 331:1081–1084PubMedGoogle Scholar
  68. Niederberger T, Hartung S, Hopfner KP, Tresch A (2011) Processive RNA decay by the exosome: merits of a quantitative Bayesian sampling approach. RNA Biol 8:55–60Google Scholar
  69. Oddone A, Lorentzen E, Basquin J, Gasch A, Rybin V, Conti E, Sattler M (2007) Structural and biochemical characterization of the yeast exosome component Rrp40. EMBO Rep 8:63–69PubMedGoogle Scholar
  70. Orban TI, Izaurralde E (2005) Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome. RNA 11:459–469PubMedGoogle Scholar
  71. Portnoy V, Schuster G (2006) RNA polyadenylation and degradation in different Archaea; roles of the exosome and RNase R. Nucleic Acids Res 34:5923–5931PubMedGoogle Scholar
  72. Portnoy V, Evguenieva-Hackenberg E, Klein F, Walter P, Lorentzen E, Klug G, Schuster G (2005) RNA polyadenylation in Archaea: not observed in Haloferax while the exosome polynucleotidylates RNA in Sulfolobus. EMBO Rep 6:1188–1193PubMedGoogle Scholar
  73. Preker P, Nielsen J, Kammler S, Lykke-Andersen S, Christensen MS, Mapendano CK, Schierup MH, Jensen TH (2008) RNA exosome depletion reveals transcription upstream of active human promoters. Science 322:1851–1854PubMedGoogle Scholar
  74. Reimer G, Scheer U, Peters JM, Tan EM (1986) Immunolocalization and partial characterization of a nucleolar autoantigen (PM-Scl) associated with polymyositis/scleroderma overlap syndromes. J Immunol 137:3802–3808PubMedGoogle Scholar
  75. Roppelt V, Hobel CF, Albers SV, Lassek C, Schwarz H, Klug G, Evguenieva-Hackenberg E (2010) The archaeal exosome localizes to the membrane. FEBS Lett 584:2791–2795PubMedGoogle Scholar
  76. Rott R, Zipor G, Portnoy V, Liveanu V, Schuster G (2003) RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli. J Biol Chem 278:15771–15777PubMedGoogle Scholar
  77. Schaeffer D, Tsanova B, Barbas A, Reis FP, Dastidar EG, Sanchez-Rotunno M, Arraiano CM, van Hoof A (2009) The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat Struct Mol Biol 16:56–62PubMedGoogle Scholar
  78. Schneider C, Leung E, Brown J, Tollervey D (2009) The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res 37:1127–1140PubMedGoogle Scholar
  79. Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS (2008) Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. RNA 14:2361–2371PubMedGoogle Scholar
  80. Slomovic S, Portnoy V, Yehudai-Resheff S, Bronshtein E, Schuster G (2008) Polynucleotide phosphorylase and the archaeal exosome as poly(A)-polymerases. Biochim Biophys Acta 1779:247–255PubMedGoogle Scholar
  81. Sohlberg B, Huang J, Cohen SN (2003) The Streptomyces coelicolor polynucleotide phosphorylase homologue, and not the putative poly(A) polymerase, can polyadenylate RNA. J Bacteriol 185:7273–7278PubMedGoogle Scholar
  82. Staals RH, Bronkhorst AW, Schilders G, Slomovic S, Schuster G, Heck AJ, Raijmakers R, Pruijn GJ (2010) Dis3-like 1: a novel exoribonuclease associated with the human exosome. EMBO J 29:2358–2367PubMedGoogle Scholar
  83. Stead JA, Costello JL, Livingstone MJ, Mitchell P (2007) The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein. Nucleic Acids Res 35:5556–5567PubMedGoogle Scholar
  84. Steitz TA, Steitz JA (1993) A general two-metal-ion mechanism for catalytic RNA. Proc Natl Acad Sci USA 90:6498–6502PubMedGoogle Scholar
  85. Symmons MF, Jones GH, Luisi BF (2000) A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure 8:1215–1226PubMedGoogle Scholar
  86. Synowsky SA, Heck AJ (2008) The yeast Ski complex is a hetero-tetramer. Protein Sci 17:119–125PubMedGoogle Scholar
  87. Takahashi S, Araki Y, Sakuno T, Katada T (2003) Interaction between Ski7p and Upf1p is required for nonsense-mediated 3′-to-5′ mRNA decay in yeast. EMBO J 22:3951–3959PubMedGoogle Scholar
  88. Taverner T, Hernandez H, Sharon M, Ruotolo BT, Matak-Vinkovic D, Devos D, Russell RB, Robinson CV (2008) Subunit architecture of intact protein complexes from mass spectrometry and homology modeling. Acc Chem Res 41:617–627PubMedGoogle Scholar
  89. Tomecki R, Dziembowski A (2010) Novel endoribonucleases as central players in various pathways of eukaryotic RNA metabolism. RNA 16:1692–1724PubMedGoogle Scholar
  90. Tomecki R, Kristiansen MS, Lykke-Andersen S, Chlebowski A, Larsen KM, Szczesny RJ, Drazkowska K, Pastula A, Andersen JS, Stepien PP et al (2010) The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L. EMBO J 29:2342–2357PubMedGoogle Scholar
  91. van Hoof A, Lennertz P, Parker R (2000a) Yeast exosome mutants accumulate 3′-extended polyadenylated forms of U4 small nuclear RNA and small nucleolar RNAs. Mol Cell Biol 20:441–452PubMedGoogle Scholar
  92. van Hoof A, Staples RR, Baker RE, Parker R (2000b) Function of the ski4p (Csl4p) and Ski7p proteins in 3′-to-5′ degradation of mRNA. Mol Cell Biol 20:8230–8243PubMedGoogle Scholar
  93. van Hoof A, Frischmeyer PA, Dietz HC, Parker R (2002) Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 295:2262–2264PubMedGoogle Scholar
  94. Walter P, Klein F, Lorentzen E, Ilchmann A, Klug G, Evguenieva-Hackenberg E (2006) Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus. Mol Microbiol 62:1076–1089PubMedGoogle Scholar
  95. Wang Z, Kiledjian M (2001) Functional link between the mammalian exosome and mRNA decapping. Cell 107:751–762PubMedGoogle Scholar
  96. Wang L, Lewis MS, Johnson AW (2005) Domain interactions within the Ski2/3/8 complex and between the Ski complex and Ski7p. RNA 11:1291–1302PubMedGoogle Scholar
  97. Wang X, Jia H, Jankowsky E, Anderson JT (2008) Degradation of hypomodified tRNA(iMet) in vivo involves RNA-dependent ATPase activity of the DExH helicase Mtr4p. RNA 14:107–116PubMedGoogle Scholar
  98. Weir JR, Bonneau F, Hentschel J, Conti E (2010) Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance. Proc Natl Acad Sci USA 107:12139–12144PubMedGoogle Scholar
  99. Whitfield TT, Sharpe CR, Wylie CC (1994) Nonsense-mediated mRNA decay in Xenopus oocytes and embryos. Dev Biol 165:731–734PubMedGoogle Scholar
  100. Wyers F, Rougemaille M, Badis G, Rousselle JC, Dufour ME, Boulay J, Regnault B, Devaux F, Namane A, Seraphin B et al (2005) Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase. Cell 121:725–737PubMedGoogle Scholar
  101. Yehudai-Resheff S, Portnoy V, Yogev S, Adir N, Schuster G (2003) Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins. Plant Cell 15:2003–2019PubMedGoogle Scholar
  102. Zanchin NI, Goldfarb DS (1999a) Nip7p interacts with Nop8p, an essential nucleolar protein required for 60 S ribosome biogenesis, and the exosome subunit Rrp43p. Mol Cell Biol 19:1518–1525PubMedGoogle Scholar
  103. Zanchin NI, Goldfarb DS (1999b) The exosome subunit Rrp43p is required for the efficient maturation of 5.8 S, 18 S and 25 S rRNA. Nucleic Acids Res 27:1283–1288PubMedGoogle Scholar
  104. Zhang X, Nakashima T, Kakuta Y, Yao M, Tanaka I, Kimura M (2008) Crystal structure of an archaeal Ski2p-like protein from Pyrococcus horikoshii OT3. Protein Sci 17:136–145PubMedGoogle Scholar
  105. Zuo Z, Rodgers CJ, Mikheikin AL, Trakselis MA (2010) Characterization of a functional DnaG-type primase in archaea: implications for a dual-primase system. J Mol Biol 397:664–676PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2011

Authors and Affiliations

  1. 1.Department of Biochemistry at the Gene CenterLudwig-Maximilians-UniversityMunichGermany
  2. 2.Center for Integrated Protein SciencesLudwig-Maximilians-UniversityMunichGermany
  3. 3.Life Sciences DivisionLawrence Berkeley National LaboratoryBerkeleyUSA

Personalised recommendations