Abstract
The phenomenon of restriction and modification (R-M) was first discovered in the early 1950s. It was observed that certain strains of bacteria inhibited (‘restricted’) the growth of bacteriophages previously propagated on a different strain. In the early 1960s, it was found that the restriction is due to the enzymatic cleavage of the phage DNA by sequence -specific endonucleases (REases), which are sensitive to covalent modification of bases in the target sequence. Some of the REases produced discrete DNAfragments upon cleavage. This property proved very useful for analyzing and rearranging DNA, which soon prompted the rapid development of genetic engineering techniques as well as the search for more REaseswith novel recognition sequences (early review: Arber and Linn 1969). It was in the mid-1970s when cloning of R-M enzymes themselves began (review by Lunnen et al. 1988). It was found that most of restriction enzymes are genetically linked with modification enzymes of cognate specificity, forming R-M systems, but a few solitary enzymes were also characterized (reviews: Wilson 1991; Wilson and Murray 199I).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Aggarwal AK (1995) Structure and function of restriction endonucleases. Curr Opin Struct Biol 5:11–19
Aravind L, Walker DR, Koonin EV (1999) Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res 27:1223–1242
Aravind L, Makarova KS, Koonin EV (2000) Holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories. Nucleic Acids Res 28:3417–3432
Arber W (1979) Promotion and limitation of genetic exchange. Science 205:361–365
Arber W (2000) Genetic variation: molecular mechanisms and impact on microbial evolution. FEMS Microbiol Rev 24:1–7
Arber W, Linn S (1969) DNAmodification and restriction. Annu Rev Biochem 38:467500
Ban C, Yang W (1998) Structural basis for MutH activation in E. coli mismatch repair and relationship of MutH to restriction endonucleases. EMBO J 17:1526–1534
Bickle TA, Kruger DH (1993) Biology of DNArestriction. Microbiol Rev 57:434–450
Bond CS, Kvaratskhelia M, Richard D, White MF, Hunter WN (2001) Structure of Hjc, a Holliday junction resolvase, from Sulfolobus solfatar icus. Proc Natl Acad Sci USA 98:5509–5514
Bozic D, Grazulis S, Siksnys V, Huber R (1996) Crystal structure of Citrobacter freundii restriction endonuclease CfrlOI at 2.15 Åresolution. J Mol Bioi 255:176–186
Bujnicki JM (2000) Phylogeny of the restriction endonuclease-like superfamily inferred from comparison of protein structures. J Mol Evol 50:39–44
Bujnicki JM (2001a) A model of structure and action of Sau3AI restriction endonuclease that comprises two MutH-like endonuclease domains within a single polypeptide. Acta Microbiol Pol 50:219–231
Bujnicki JM (2001b) Understanding the evolution of restriction-modification systems: clues from sequence and structure comparisons. Acta Biochim Pol 48:1–33
Bujnicki JM (2003) Crystallographic and bioinformatics studies on restriction endonucleases: inference of evolutionary relationships in the ‘midnight zone’ of homology. Curr Prot Pept Sci 4 (in press)
Bujnicki JM, Rychlewski L (2001a) Grouping together highly diverged PD-(D/E)XK nucleases and identification of novel superfamily members using structure-guided alignment of sequence profiles. J Mol Microbiol Biotechnol 3:69–72
Bujnicki JM, Rychlewski L (2001b) Identification of a PD-(D/E)XK-like domain with a novel configuration of the endonuclease active site in the methyl-directed restriction enzyme Mrr and its homologs. Gene 267:183–191
Bujnicki JM, Rychlewski L (2001c) The herpesvirus alkaline exonuclease belongs to the restriction endonuclease PD-(D/E)XK superfamily: insight from molecular modeling and phylogenetic analysis. Virus Genes 22:219–230
Bujnicki JM, Rychlewski L (2001d) Unusual evolutionary history of the tRNA splicing endonuclease EndA: relationship to the LAGLIDADG and PD-(D/E)XK deoxyribonucleases. Protein Sci 10:656–660
Bujnicki JM, Radlinska M, Rychlewski L (2000) Atomic model of the 5-methylcytosinespecific restriction enzyme McrA reveals an atypical zinc-finger and structural similarity to ββαMe endonucleases. Mol Microbiol 37:1280–1281
Bujnicki JM, Radlinska M, Rychlewski L (2001a) Polyphyletic evolution of Type II restriction enzymes revisited: two independent sources of second-hand folds revealed. Trends Biochem Sci 26:9–11
Bujnicki JM, Rotkiewicz P, Kolinski A, Rychlewski L (2001b) Three-dimensional modeling of the I-TevI homing endonuclease catalytic domain, a GIY-YIG member, using NMR restraints and Monte Carlo dynamics. Protein Eng 14:717–21
Carlson K, Kosturko LD (1998) Endonuclease II of coliphage T4: a recombinase disguised as a restriction endonuclease? Mol Microbiol 27:671–676
Carugo O, Pongor S (2002) Protein fold similarity estimated by a probabilistic approach based on Cα-Cα distance comparison. J Mol Biol 315:887–898
Chang HW, Julin DA (2001) Structure and function of the Escherichia coli RecE protein, a member of the RecB nuclease domain family. J Biol Chern 276:46004–46010
Cheng X, Balendiran K, Schildkraut I, Anderson JE (1994) Structure of PvuII endonuclease with cognate DNA. EMBO J 13:3927–3935
Chinen A, Uchiyama I, Kobayashi I (2000) Comparison between Pyrococcus horikoshii and Pyrococcus abyssi genome sequences reveals linkage of restriction-modification genes with large genome polymorphisms. Gene 259:109–121
Daiyasu H, Komori K, Sakae S, Ishino Y, Toh H (2000) Hjc resolvase is a distantly related member of the Type II restriction endonuclease family. Nucleic Acids Res 28:4540–4543
Davies GP, Kemp P, Molineux IJ, Murray NE (1999a) The DNA translocation and ATPase activities of restriction-deficient mutants of EcoKI. J Mol Biol 292:787–796
Davies GP, Martin I, Sturrock SS, Cronshaw A, Murray NE, Dryden DT (1999b) On the structure and operation of Type I DNA restriction enzymes. J Mol Biol 290:565–579
Deibert M, Grazulis S, Janulaitis A, Siksnys V, Huber R (1999) Crystal structure of MunI restriction endonuclease in complex with cognate DNA at 1.7 A resolution. EMBO J 18:5805–5816
Deibert M, Grazulis S, Sasnauskas G, Siksnys V, Huber R (2000) Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA. Nat Struct Biol 7:792–799
Finnegan DJ (1997) Transposable elements: how non-LTR retrotransposons do it. Curr Biol 7:R245–R248
Friedhoff P, Lurz R, Luder G, Pingoud A (2001) Sau3AI. a monomeric Type II restriction endonuclease that dimerizes on the DNA and thereby induces dna loops. J Biol Chern 276:23581–23588
Fuxreiter M, Simon I (2002) Protein stability indicates divergent evolution of PD-(D/E) XK Type II restriction endonucleases. Protein Sci 11:1978–1983
Gimble FS (2000) Invasion of a multitude of genetic niches by mobile endonuclease genes. FEMS Microbiol Lett 185:99–107
Grazulis S, Deibert M, Rimseliene R, Skirgaila R, Sasnauskas G, Lagunavicius A, Repin V, Urbanke C, Huber R, Siksnys V (2002) Crystal structure of the Bse634I restriction endonuclease: comparison of two enzymes recognizing the same DNA sequence. Nucleic Acids Res 30:876–885
Grishin NV (1997) Estimation of evolutionary distances from protein spatial structures. J Mol EvoI 45:359–369
Grishin NV (2001) Fold change in evolution of protein structures. J Struct Biol 134:167–185
Hadden JM, Convery MA, Declais AC, Lilley DM, Phillips SE (2001) Crystal structure of the Holliday junction resolving enzyme T7 endonuclease I. Nat Struct Biol 8:62–67
Hasson MS, Schlichting I, Moulai J, Taylor K, Barrett W, Kenyon GL, Babbitt PC, Gerlt JA, Petsko GA, Ringe D (1998) Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase. Proc Natl Acad Sci USA 95:10396–10401
Heitman J (1993) On the origins, structures and functions of restriction-modification enzymes. Genet Eng N Y 15:57–108
Hickman AB, Li Y, Mathew SV, May EW, Craig NL, Dyda F (2000) Unexpected structural diversity in DNA recombination: the restriction endonuclease connection. Mol Cell 5:1025–1034
Horton NC, Dorner LF, Perona JJ (2002) Sequence selectivity and degeneracy of a restriction endonuclease mediated by DNAintercalation. Nat Struct Biol 9:42–47
Huai Q, Colandene JD, Chen Y, Luo F, Zhao Y, Topal MD, Ke H (2000) Crystal structure of NaeI-an evolutionary bridge between DNAendonuclease and topoisomerase. EMBO J 19:3110–3118
Huai Q, Colandene JD, Topal MD, Ke H (2001) Structure of NaeI-DNA complex reveals dual-mode DNA recognition and complete dimer rearrangement. Nat Struct Biol 8:665–669
Ichiyanagi K, Ishino Y, Ariyoshi M, Komori K, Morikawa K (2000) Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI. J Mol Bioi 300:889–901
Iyer LM, Koonin EV, Aravind L (2002) Extensive domain shuffling in transcription regulators of DNAviruses and implications for the origin of fungal APSES transcription factors. Genome BioI 3:RESEARCHOOI2
Janosi L, Yonemitsu H, Hong H, Kaji A (1994) Molecular cloning and expression of a novel hydroxymethylcytosine-specific restriction enzyme (PvuRtslI) modulated by glucosylation of DNA. J Mol Bioi 242:45–61
Janscak P, Sandmeier U, Bickle TA (1999) Single amino acid substitutions in the HsdR subunit of the Type IB restriction enzyme EcoAI uncouple the DNA translocation and DNAcleavage activities of the enzyme. Nucleic Acids Res 27:2638–2643
Janscak P, Sandmeier U, Szczelkun MD, Bickle TA (2001) Subunit assembly and mode of DNA cleavage of the Type III restriction endonucleases EcoPlI and EcoP151. J Mol Bioi 306:417–431
Jeltsch A, Kroger M, Pingoud A (1995) Evidence for an evolutionary relationship among type-II restriction endonucleases. Gene 160:7–16
Jeltsch A, Pingoud A (1996) Horizontal gene transfer contributes to the wide distribution and evolution of Type II rest riction-modification systems. J Mol Evol 42:91–96
Johnson MS, Sutcliffe MJ, Blundell TL (1990) Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins. J Mol Evol 30:43–59
Jurica MS, Stoddard BL (1999) Homing endonucleases: structure, function and evolution. Cell Mol Life Sci 55:1304–1326
Jurica MS, Monnat RJJ, Stoddard BL (1998) DNArecognition and cleavage by the LAGLIDADGhoming endonuclease I-Crel. Mol Cell 2:469–476
Kim Y, Grable JC, Love R, Green PJ, Rosenberg JM (1990) Refinement of EcoRI endonuclease crystal structure: a revised protein chain tracing. Science 249:1307–1309
Kinch LN, Grishin NV (2002) Evolution of protein structures and functions. Curr Opin Struct Biol 12:400–408
Kobayashi I (2001) Behavior of restriction-modification systems as selfish mobile elements and their impact on genome evolution. Nucleic Acids Res 29:3742–3756
Kong H, Lin LF, Porter N, Stickel S, Byrd D, Posfai J, Roberts RJ (2000) Functional analysis of putative restriction-modification system genes in the Helicobacter pylori J99 genome. Nucleic Acids Res 28:3216–3223
Kostrewa D, Winkler FK (1995) Mg2+ binding to the active site of EcoRVendonuclease: a crystallographic study of complexes with substrate and product DNA at 2 Åresolution. Biochemistry 34:683–696
Kovall RA, Matthews BW (1998) Structural, functional, and evolutionary relationships between lambda-exonuclease and the Type II restriction endonucleases. Proc Natl Acad Sci USA 95:7893–7897
Kowalski JC, Belfort M, Stapleton MA, Holpert M, Dansereau JT, Pietrokovski S, Baxter SM, Derbyshire V (1999) Configuration of the catalytic GIY-YIG domain of intron endonuclease I-TevI: coincidence of computational and molecular findings. Nucleic Acids Res 27:2115–2125
Kruger DH, Bickle TA (1983) Bacteriophage survival: multiple mechanisms for avoiding the deoxyribonucleic acid restriction systems of their hosts. Microbiol Rev 47:345–360
Kvaratskhelia M, Wardleworth BN, Norman DG, White MF (2000) A conserved nuclease domain in the archaeal holliday junction resolving enzyme Hjc. J Biol Chern 275:25540–25546
Lagunavicius A, Siksnys V (1997) Site-directed mutagenesis of putative active site residues of MunI restriction endonuclease: replacement of catalytically essential carboxylate residues triggers DNAbinding specificity. Biochemistry 36:11086–11092
Lagunavicius A, Sasnauskas G, Halford SE, Siksnys V (2003) The metal-independent Type lIS restriction enzyme BfiI is a dimer that binds two DNAsites but has only one catalytic centre. J Mol Biol 326(4):1051–64
Li H, Abelson (2000) Crystal structure of a dimeric archaeal splicing endonuclease. J Mol Biol 302:639–648
Li H, Trotta CR, Abelson J (1998) Crystal structure and evolution of a transfer RNAsplicing enzyme. Science 280:279–284
Lin LF, Posfai J, Roberts RJ, Kong H (2001) Comparative genomics of the restrictionmodification systems in Helicobacter pylori. Proc Natl Acad Sci USA 98:2740–2745
Lukacs CM, Kucera R, Schildkraut I, Aggarwal AK (2000) Understanding the immutability of restriction enzymes: crystal structure of BglII and its DNA substrate at 1.5 Å resolution. Nat Struct Biol 7:134–140
Lunnen KD, Barsomian JM, Camp RR, Card CO, Chen SZ, Croft R, Looney MC, Meda MM, Moran LS, Nwankwo DO (1988) Cloning type-II restriction and modification genes. Gene 74:25–32
Luria SE, Human ML (1952) A nonhereditary, host-induced variation of bacterial viruses. J Bacteriol 64:557–569
Martin JL (1995) Thioredoxin-a fold for all reasons. Structure 3:245–250
Matveyev AV, Young KT, Meng A, Elhai J (2001) DNAmethyltransferases of the cyanobacterium Anabaena PCC 7120. Nucleic Acids Res 29:1491–1506
May AC (1999) Toward more meaningful hierarchical classification of protein threedimensional structures. Proteins 37:20–29
McClarin JA, Frederick CA, Wang BC, Greene P, Boyer HW, Grable J, Rosenberg JM (1986) Structure of the DNA-Eco RI endonuclease recognition complex at 3 Aresolution. Science 234:1526–1541
Morgan RD, Xiao JP, Xu SY (1998) Characterization of an extremely thermostable restriction enzyme, PspGI, from a Pyrococcus strain and cloning of the PspGI restriction-modification system in Escherichia coli. Appl Environ Microbiol 64:3669–3673
Mucke M, Grelle G, Behlke J, Kraft R, Kruger DH, Reuter M (2002) EcoRII: a restriction enzyme evolving recombination functions? EMBO J 21:5262–5268
Murzin AG (1998) How far divergent evolution goes in proteins. Curr Opin Struct Biol 8: 380–387
Murzin AG, Brenner SE, Hubbard T, Chothia C (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247:536–540
Nastri HG, Evans PD, Walker IH, Riggs PD (1997) Catalytic and DNAbinding properties of Pvull restriction endonuclease mutants. J Biol Chern 272:25761–25767
Nei M (1996) Phylogenetic analysis in molecular evolutionary genetics. Annu Rev Genet 30:371–403
Newman M, Lunnen K, Wilson G, Greci J, Schildkraut I, Phillips SE (1998) Crystal structure of restriction endonuclease BglI bound to its interrupted DNA recognition sequence. EMBO J 17:5466–5476
Newman M, Strzelecka T, Dorner LF, Schildkraut I, Aggarwal AK (1994) Structure of restriction endonuclease BamHI and its relationship to EcoRI. Nature 368:660–664
Nishino T, Komori K, Tsuchiya D, Ishino Y, Morikawa K (2001) Crystal structure of the Archaeal Holliday junction resolvase Hjc and implications for DNA recognition. Structure 9:197–204
Nobusato A, Uchiyama I, Kobayashi I (2000a) Diversity of restriction-modification gene homologues in Helicobacter pylori. Gene 259:89–98
Nobusato A, Uchiyama I, Ohashi S, Kobayashi I (2000b) Insertion with long target duplication: a mechanism for gene mobility suggested from comparison of two related bacterial genomes. Gene 259:99–108
Nolling J, de Vos WM (1992) Characterization of the archaeal, plasmid-encoded Type II restriction-modification system Mth’I’I from Methanobacterium thermoformicicum THF: homology to the bacterial NgoPiII system from Neisseria gonorrhoeae. J Bacteriol 174: 5719–5726
Pingoud A, Jeltsch A (1997) Recognition and cleavage of DNA by type-II restriction endonucleases. Eur J Biochem 246:1–22
Pingoud A, Jeltsch A (2001) Structure and function of Type II restriction endonucleases. Nucleic Acids Res 29:3705–3727
Pingoud V, Kubareva E, Stengel G, Friedhoff P, Bujnicki JM, Urbanke C, Sudina A, Pingoud A (2002) Evolutionary relationship between different subgroups of restriction endonucleases. J BioI Chern 277:14306–14314
Reuter M, Schneider-Mergener J, Kupper D, Meisel A, Mackeldanz P, Kruger DH, Schroeder C (1999) Regions of endonuclease EcoRII involved in DNAtarget recognition identified by membrane-bound peptide repertoires. J BioI Chern 274:5213–5221
Rigden DJ, Setlow P, Setlow B, Bagyan I, Stein RA, Iedrzejas MJ (2002) PrfA protein of Bacillus species: prediction and demonstration of endonuclease activity on DNA. Protein Sci 11:2370–2381
Roberts RJ, Macelis D (2001) REBASE-restriction enzymes and methylases. Nucleic Acids Res 29:268–269
Roberts RJ, Belfort M, Bestor T, Bhagwat AS, Bickle TA, Bitinaite J, Blumenthal RM, Degtyarev SK, Dryden DT, Dybvig K, Firman K, Gromova ES, Gumport RI, Halford SE, Hattman S, Heitman J, Hornby DP, Janulaitis A, Jeltsch A, Josephsen J, Kiss A, Iaenhammer T, Kobayashi I, Kong H, Kruger D, Lacks S, Marinus MG, Miyahara M, Morgan RD, Murray NE, Nagaraja V, Piekarowicz A, Pingoud A, Raleigh E, Rao DN, Reich N, Repin V, Selker E, Shaw PC, Stein DC, Stoddard BL, Szybalski W, Trautner TA, Van Etten JL, Vitor JM, Wilson GG, Xu SY (2003a) Anomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes. Nucleic Acids Res 31(7):1805–1812
Roberts RJ, Vincze T, Posfai J, Macelis D (2003b) REBASE: restriction enzymes and methyltransferases. Nucleic Acids Res 31:418–420
Rocha EP, Danchin A, Viari A (2001) Evolutionary role of restriction/modification systems as revealed by comparative genome analysis. Genome Res 11:946–958
Rost B (1997) Protein structures sustain evolutionary drift. Fold Des 2:S19–S24
Rost B (2002) Enzyme function less conserved than anticipated. J Mol Biol 318:595–608
Sapranauskas R, Sasnauskas G, Lagunavicius A, Vilkaitis G, Lubys A, Siksnys V (2000) Novel subtype of Type Ils restriction enzymes. J Biol Chern 275:30878–30885
Siksnys V, Zareckaja N, Vaisvila R, Timinskas A, Stakenas P, Butkus V, Janulaitis A (1994) CAATTG-specific restriction-modification MunI genes from Mycoplasma: sequence similarities between R.MunI and R.EcoRI. Gene 142:1–8
Siksnys V, Timinskas A, Klimasauskas S, Butkus V, Janulaitis A (1995) Sequence similarity among type-II restriction endonucleases, related by their recognized 6-bp target and tetranucleotide-overhang cleavage. Gene 157:311–314
Silva GH, Dalgaard JZ, Belfort M, Van Roey P (1999) Crystal structure of the thermostable archaeal intron-encoded endonuclease I-DmoI. J Mol Biol 286:1123–1136
Skirgaila R, Grazulis S, Bozic D, Huber R, Siksnys V (1998) Structure-based redesign of the catalytic/metal binding site of Cfrl0I restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues. J Mol Biol 279:473–481
Stephenson FH, Ballard BT, Boyer HW, Rosenberg JM, Greene PJ (1989) Comparison of the nucleotide and amino acid sequences of the RsrI and EcoRI restriction endonucleases. Gene 85:1–13
Tamulaitis G, Solonin AS, Siksnys V (2002) Alternative arrangements of catalytic residues at the active sites of restriction enzymes. FEBS Lett 518:17–22
Thielking V, Selent U, Kohler E, Wolfes H, Pieper U, Geiger R, Urbanke C, Winkler FK, Pingoud A (1991) Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis. Biochemistry 30:6416–6422
Todd AE, Orengo CA, Thornton JM (2001) Evolution of function in protein superfamilies, from a structural perspective. J Mol Biol 307:1113–1143
Todone F, Weinzierl RO, Brick P, Onesti S (2000) Crystal structure of RPB5, a universal eukaryotic RNApolymerase subunit and transcription factor interaction target. Proc Nat! Acad Sci USA 97:6306–6310
Tsutakawa SE, Jingarni H, Morikawa K (1999a) Recognition of a TG mismatch: the crystal structure of very short patch repair endonuclease in complex with a DNA duplex. Cell 99:615–623
Tsutakawa SE, Muto T, Kawate T, Jingami H, Kunishima N, Ariyoshi M, Kohda D, Nakagawa M, Morikawa K (1999b) Crystallographic and functional studies of very short patch repair endonuclease. Mol Cell 3:621–628
van der Woerd MJ, Pelletier JJ, Xu S, Friedman AM (2001) Restriction enzyme BsoBIDNA complex: a tunnel for recognition of degenerate DNA sequences and potential histidine catalysis. Structure (Camb) 9:133–144
Van Roey P, Meehan L, Kowalski JC, Belfort M, Derbyshire V (2002) Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI. Nat Struct Biol 9:806–811
Venclovas C, Timinskas A, Siksnys V (1994) Five-stranded beta-sheet sandwiched with two alpha-helices: a structural link between restriction endonucleases EcoRI and EcoRV. Proteins 20:279–282
Viadiu H, Aggarwal AK (1998) The role of metals in catalysis by the restriction endonuclease BamHI. Nat Struct Biol 5:910–916
Wah DA, Hirsch JA, Dorner LF, Schildkraut I, Aggarwal AK (1997) Structure of the multimodular endonuclease FokI bound to DNA. Nature 388:97–100
Wang J, Chen R, Julin DA (2000) A single nuclease active site of the Escherichia coli RecBCDenzyme catalyzes single-stranded DNA degradation in both directions. J Biol Chern 275:507–513
Wilson GG (1991) Organization of restriction-modification systems. Nucleic Acids Res 19:2539–2566
Wilson GG, Murray NE (1991) Restriction and modification systems. Annu Rev Genet 25:585–627
Winkler FK, Banner DW, Oefner C, Tsernoglou D, Brown RS, Heathman SP, Bryan RK, Martin PD, Petratos K, Wilson KS (1993) The crystal structure of EcoRVendonuclease and of its complexes with cognate and non-cognate DNA fragments. EMBO J 12:1781–1795
Withers BE, Ambroso LA, Dunbar JC (1992) Structure and evolution of the XcyI restriction-modification system. Nucleic Acids Res 20:6267–6273
Xu Y, Lunnen KD, Kong H (2001) Engineering a nicking endonuclease N.AlwIby domain swapping. Proc Natl Acad Sci USA 98:12990–12995
Yang J, Malik HS, Eickbush TH (1999) Identification of the endonuclease domain encoded by R2 and other site-specific, non-long terminal repeat retrotransposable elements. Proc Natl Acad Sci USA 96:7847–7852
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2004 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Bujnicki, J.M. (2004). Molecular Phylogenetics of Restriction Endonucleases. In: Pingoud, A.M. (eds) Restriction Endonucleases. Nucleic Acids and Molecular Biology, vol 14. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-18851-0_3
Download citation
DOI: https://doi.org/10.1007/978-3-642-18851-0_3
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-62324-0
Online ISBN: 978-3-642-18851-0
eBook Packages: Springer Book Archive