Cited by 714Genomics and Phylogenetic StudiesChromosomal and Genetic VariationsGenome Rearrangement Algorithms

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RESTRICTION AND MODIFICATION SYSTEMS

Wilson, Geoffrey G., Murray, Noreen E.·1991·Annual Review of Genetics

DOI 10.1146/annurev.ge.25.120191.003101

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Abstract

Orthologs and paralogs are two fundamentally different types of homologous genes that evolved, respectively, by vertical descent from a single ancestral gene and by duplication. Orthology and paralogy are key concepts of evolutionary genomics. A ...Read More

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Crossref · 10.1146/annurev.ge.25.120191.003101

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DNA Restriction Enzyme from E. coli
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McrA and McrB restriction phenotypes of someE.colistrains and implications for gene cloning
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Self-citation
DNA Restriction and Modification Mechanisms in Bacteria
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“for the survival of the organism) (26).”
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“influenzae, and in Salmonella and Citrobacter (Wilson and Murray 1991).”
BackgroundInfluential
Structure of the restriction–modification controller protein C.Esp1396I
Ball, N. J., Streeter, S. D., Kneale, G. G., & McGeehan, J. E. (2009) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909020514 · Cited by 16
“M system allows the discrimination of ‘self’ from ‘nonself’ DNA (Wilson & Murray, 1991).”
Background
Characterization of a Novel Plasmid-Encoded HsdS Subunit, S.LlaW12I, from Lactococcus lactis W12
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POLYMORPHISM OF BACTERIAL RESTRICTION‐MODIFICATION SYSTEMS: THE ADVANTAGE OF DIVERSITY
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DNA Binding and Subunit Interactions in the Type I Methyltransferase M.EcoR124I
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Surface Labelling of the Type I Methyltransferase M.EcoR124I Reveals Lysine Residues Critical for DNA Binding
Taylor, I. A., Webb, M., & Kneale, G. G. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0234 · Cited by 16
“Type I methyltransferases (MTases) are more complex enzymes ( Wilson & Murray, 1991; Bickle & Kruger, 1993), having separate subunits for DNA recognition (HsdS) and methyltransferase activity (HsdM).”
Background
Sequence Comparison of the EcoHK31I and EaeI. Restriction-Modification Systems Suggests an Intergenic Transfer of Genetic Material
Lee, C., Shaw, P., Picone, S. J., Wilson, G. G., & Lunnen, K. D. (1998) · Biological Chemistry · doi:10.1515/bchm.1998.379.4-5.437 · Cited by 16
“In contrast, DNA methyltransferases (MTases) share conserved motifs (Posfai ef a/., 1989; Wilson and Murray, 1991).”
BackgroundSelf-citation
Cloning and sequence comparison of
Ruan, H., Lunnen, K. D., Scott, M. E., Moran, L. S., Slatko, B. E., Pelletier, J. J., Hess, E. J., Benner, J. S., Wilson, G. G., & Xu, S.-Y. (1996) · Molecular and General Genetics MGG · doi:10.1007/s004380050278 · Cited by 16
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Processing DNA molecules as text
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“A common technique is the use of restriction enzymes to cut the DNA molecule at speciﬁc sites which enables the joining of DNA fragments that contains matching sites on their ends (Wilson 1988; Wilson and Murray 1991).”
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“To reduce the risk of acquisition of exogenous DNA, prokaryotes have evolved both innate immunity that is mediated by restriction-modification systems (4) and adaptive immunity that is mediated by CRISPR-Cas systems (5–13).”
Background
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“Several such defense mechanisms have been discussed in the literature, including the restriction–modification system (RM) [79] and envelope resistance [80].”
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“They are usually accompanied by DNA methyltransferases (MTases) of similar specificity, which methylate the DNA of the host, thereby rendering it resistant to the cleavage (Wilson and Murray 1991).”
Background
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“The simplest systems are type II R-M systems, which usually consist of two separate enzymes, a restriction endonuclease and a methyltransferase (4, 40).”
Background
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“Restriction-Modification (RM) systems use two enzyme activities to defend bacteria against foreign DNA, a restriction endonuclease (REase) and a modification methyltransferase (MTase) (1,2).”
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“Type II restriction–modification (R–M) systems encode a restriction endonuclease that recognizes and cleaves specific DNA sequences and a methyltransferase that recognizes the same DNA sequence and methylates it first on one DNA strand - to produce hemimethylated DNA - and then on the other strand to produce fully met…”
Background
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Characterization of DNA binding activities of over-expressedKpnI restriction endonuclease and modification methylase
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“Most of the enzymes of this group recognize palindromic sequence which generally vary between four to eight base pairs in length ( Wilson and Murray 1991 ).”
Background
The NIaIV restriction and modification genes of Neisseria lactamica are flanked by leucine biosynthesis genes
Lau, P. C. K., Forghani, F., Labbé, D., Bergeron, H., Brousseau, R., & Höltke, H.-J. (1994) · Molecular and General Genetics MGG · doi:10.1007/bf00283872 · Cited by 14
“1989) are typically found within a polypeptide ranging from 228 to 587 amino acids in length (Wilson and Murray 1991).”
BackgroundInfluential
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“This system displays similarities to methylation-based R-M systems [9,10,11,12].”
Method
The Type ISP Restriction-Modification enzymes LlaBIII and LlaGI use a translocation-collision mechanism to cleave non-specific DNA distant from their recognition sites
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“The Restriction–Modification (RM) enzymes play an important role in bacteria and archaea by preventing infection by bacteriophages and other foreign DNA elements (1,2).”
Background
Giant Chlorella Viruses
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Sequence-specific DNA Recognition by the SmaI Endonuclease
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“, StySBLI), based on genetic complementation, cross-hybridization of genes, and antibody cross-reactivity [6,7].”
Background
Cloning and characterization of the unusual restriction-modification system comprising two restriction endonucleases and one methyltransferase
Stankevicius, K., Povilionis, P., Lubys, A., Menkevičius, S., & Janulaitis, A. (1995) · Gene · doi:10.1016/0378-1119(94)00796-u · Cited by 14
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The elastic network model reveals a consistent picture on intrinsic functional dynamics of type II restriction endonucleases
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Recognition of dual symmetry by the controller protein C.Esp1396I based on the structure of the transcriptional activation complex
McGeehan, J. E., Ball, N. J., Streeter, S. D., Thresh, S.-J., & Kneale, G. G. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1250 · Cited by 13
“The sequencespecific DNA methyltransferase protects the host DNA from cleavage by the associated restriction enzyme, and the specific methylation pattern of the host RM system allows the discrimination of ‘self’ from ‘non-self’ DNA (2).”
Evidence for the existence of a restriction-modification system common to several species of the family Vibrionaceae
Matsuzaki, S., Inoue, T., & Tanaka, S. (1992) · FEMS Microbiology Letters · doi:10.1016/0378-1097(92)90607-p · Cited by 13
Transmission barrier of the bla KPC plasmid mediated by type I restriction-modification systems in Escherichia coli
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Biological Codes: A Field Guide for Code Hunters
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“Historically, restriction-modification endonucleases have been and continue to be used as tools for gene cloning (Wilson and Murray 1991 ) and have enabled many of the achievements of modern biology, while whole bacteriophages have become biotechnological tools in their own right (Elois et al.…”
Structural Insights into the Assembly and Shape of Type III Restriction–Modification (R–M) EcoP15I Complex by Small-Angle X-ray Scattering
Gupta, Y. K., Yang, L., Chan, S., Samuelson, J. C., Xu, S.-Y., & Aggarwal, A. K. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.04.026 · Cited by 12
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Striking Bimodal Methylation of the Repeat Unit of the Tandem Array Encoding Human U2 snRNA (the RNU2 Locus)
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“In prokaryotes, DNA methylation plays an essential role in the host defense mechanism against foreign DNA invasion as part of the restriction modification systems ( Wilson and Murray, 1991 ).”
Background
Transfer of megaplasmid pKB1 from the rubber-degrading bacterium Gordonia westfalica strain Kb1 to related bacteria and its modification
Bröker, D., Arenskötter, M., & Steinbüchel, A. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1262-8 · Cited by 12
“Possibly, these strains possess a highly efficient protection system against foreign DNA, such as restriction–modification (R–M) systems (Wilson and Murray 1991), a histonelike nucleoid structure-like (H-NS) protein repression system (Navarre et al.”
Background
Interaction of the type I methyltransferase M.EcoR124I with modified DNA substrates: sequence discrimination and base flipping
Mernagh, D., Taylor, I. A., & Kneale, G. G. (1998) · Biochemical Journal · doi:10.1042/bj3360719 · Cited by 12
[23] Characterization of type II DNA-methyltransferases
Landry, D., Barsomian, J. M., Feehery, G. R., & Wilson, G. G. (1992) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(92)16025-f · Cited by 12
Self-citation
Reappraisal of the DNA phosphorothioate modification machinery: uncovering neglected functional modalities and identification of new counter-invader defense systems
Rakesh, S., Aravind, L., & Krishnan, A. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkad1213 · Cited by 11
“In conventional R-M systems, this domain plays a key role in the recognition of their target DNA sequence motifs ( 3 , 4 , 70 , 71 ).”
Background
Advances in Diversity, Evolutionary Dynamics and Biotechnological Potential of Restriction-Modification Systems
Chen, C., Zhang, Y., Wu, H., Qiao, J., & Caiyin, Q. (2025) · Microorganisms · doi:10.3390/microorganisms13051126 · Cited by 12
Structural Analysis of a Novel Class of R–M Controller Proteins: C.Csp231I from Citrobacter sp. RFL231
McGeehan, J. E., Streeter, S. D., Thresh, S.-J., Taylor, J. E. N., Shevtsov, M. B., & Kneale, G. G. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.033 · Cited by 11
“Bacterial restriction–modification (R–M) systems employ a range of mechanisms for the temporal regulation of methylase and restriction endonuclease.(1) In many type II systems, this is achieved at the transcriptional level by the action of a small helix–turn–helix controller protein, or C-protein.”
Forensics: Food Authentication Using MtDNA
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“Three types of restriction modification RM (type I, II and III) have been found and were classified according to their subunit composition, cofactor requirement and mode of action [94].”
EcoR124I: from Plasmid-Encoded Restriction-Modification System to Nanodevice
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Isolation and Characterization of a HpyC1I Restriction-Modification System in Helicobacter pylori
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Circular permutation of DNA cytosine-N4 methyltransferases: in vivo coexistence in the BcnI system and in vitro probing by hybrid formation
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SruI restriction endonuclease from Selenomonas ruminantium
Vanat, I., PristaÅ¡, P., RyboÅ¡ovÃ¡l, E., Godány, A., & Javorský, P. (1993) · FEMS Microbiology Letters · doi:10.1016/0378-1097(93)90257-3 · Cited by 11
TstI, a Type II restriction–modification protein with DNA recognition, cleavage and methylation functions in a single polypeptide
Smith, R. M., Pernstich, C., & Halford, S. E. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku187 · Cited by 10
“In contrast, Type II RM systems generally feature two separate proteins, for restriction and modification respectively (6).”
The Fsp4HI restriction-modification system: Gene cloning, comparison of protein structures, and biochemical properties of recombinant DNA methyltransferase M.Fsp4HI
Chmuzh, E. V., Kashirina, Y. G., Tomilova, Y. E., Chernukhin, V. A., Okhapkina, S. S., Gonchar, D. A., Dedkov, V. S., Abdurashitov, M. A., & Degtyarev, S. K. (2007) · Molecular Biology · doi:10.1134/s0026893307010062 · Cited by 10
“MT modifies certain bases within the recognition sites of the host DNA, thereby protecting it from digestion by cognate RE [1, 2].”
Background
Differences in Methylation at GATC Sites in Genomic DNA of Campylobacter coli from Turkeys and Swine
Wright, S., Simone, W., Miller, W. G., Mandrell, R. E., Siletzky, R. M., & Kathariou, S. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00934-10 · Cited by 10
“bacterial genomes and is frequently associated with restrictionmodification systems (30).”
Background
Organization of the BcgI restriction–modification protein for the transfer of one methyl group to DNA
Smith, R. M., Jacklin, A. J., Marshall, J. J. T., Sobott, F., & Halford, S. E. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1000 · Cited by 10
“Many Type II systems have palindromic recognition sites, with the same 50–30 sequence in both strands (3).”
BackgroundInfluential
Application of methylation in improving plasmid transformation into Helicobacter pylori
Zhao, H., Xu, L., Rong, Q., Xu, Z., Ding, Y., Zhang, Y., Wu, Y., Li, B., & Ji, X. (2018) · Journal of Microbiological Methods · doi:10.1016/j.mimet.2018.05.016 · Cited by 10
Bacteria-Phage Antagonistic Coevolution and the Implications for Phage Therapy
Brockhurst, M. A., Koskella, B. L., & Zhang, Q. (2021) · Springer eBooks · doi:10.1007/978-3-319-41986-2_7 · Cited by 10
Dimeric/oligomeric DNA methyltransferases: an unfinished story
Malygin, E. G., Evdokimov, A. A., & Hattman, S. (2009) · Biological Chemistry · doi:10.1515/bc.2009.082 · Cited by 10
“Thus, the paradigm was extended to include all DNA MTases except the more complex bifunctional type I and type III enzymes (Wilson and Murray, 1991; Noyer-Weidner and Trautner, 1993), which will not be considered in this review.”
Background
Starter Cultures: Bacteriophage
McGrath, S., Fitzgerald, G. F., & van Sinderen, D. (2004) · Cheese · doi:10.1016/s1874-558x(04)80067-8 · Cited by 10
Domain structure and subunit interactions in the type I DNA methyltransferase M.EcoR124I
Smith, M. A., Read, C. M., & Kneale, G. G. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5123 · Cited by 10
Are there two DNA methyltransferase gene families in plant cells? A new potential methyltransferase gene isolated from anArabidopsis thalianagenomic library
Scheidt, G., Weber, H. H., Graessmann, M., & Graessmann, A. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.6.953 · Cited by 10
Retracted
Correlation between insertion mutant activities and amino acid sequence identities of the TaqI and TthHB8 restriction endonucleases
Barany, F., & Zebala, J. A. (1992) · Gene · doi:10.1016/0378-1119(92)90297-3 · Cited by 10
Horizontal transfer and phylogenetic distribution of the immune evasion factor tarP
Gerlach, D., Sieber, R. N., Larsen, J., Krusche, J., Castro, C. D., Baumann, J., Molinaro, A., & Peschel, A. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.951333 · Cited by 9
“aureus (Waldron and Lindsay, 2006); the DNA methyltransferase HsdM; and HsdS that confers specificity via two DNA target recognition domains to HsdR, and HsdM in a clonal complex-specific manner (Wilson and Murray, 1991).”
Background
Historical Aspects of Restriction Endonucleases as Intelligent Scissors for Genetic Engineering
Alekseeva, I. V., & Kuznetsov, N. A. (2023) · Fermentation · doi:10.3390/fermentation9100874 · Cited by 10
“In contrast, their amino acid sequences are only 19% identical [11].”
Chapter 3 DNA methylation
ADAMS, R. L. P. (1996) · Principles of medical biology · doi:10.1016/s1569-2582(96)80107-3 · Cited by 9
Cloning and characterization of the TneDI restriction–modification system of Thermotoga neapolitana
Xu, Z., Han, D., Cao, J., & Saini, U. (2011) · Extremophiles · doi:10.1007/s00792-011-0397-9 · Cited by 9
“(Wilson and Murray 1991; Roberts et al. 2003).”
Background
Functional screening of a soil metagenome for DNA endonucleases by acquired resistance to bacteriophage infection
Mtimka, S., Pillay, P., Rashamuse, K. J., Gildenhuys, S., & Tsekoa, T. L. (2019) · Molecular Biology Reports · doi:10.1007/s11033-019-05137-3 · Cited by 9
“Type I enzymes have been difficult to characterize [43], because the cleave at a sites remote the recognition site [33, 39, 44, 45].”
Background
Crystallization and preliminary X-ray analysis of the controller protein C.AhdI fromAeromonas hydrophilia
McGeehan, J. E., Streeter, S. A., Cooper, J. B., Mohammed, F., Fox, G. C., & Kneale, G. G. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444903026143 · Cited by 9
“Bacterial restriction-modi®cation (RM) systems are gene complexes that allow bacteria to methylate and protect their own DNA whilst cleaving and eliminating unmethylated, i.e. foreign, DNA (Wilson & Murray, 1991; Roberts et al., 2003).”
BackgroundInfluential
Characterisation of a complex restriction/modification system detected in a Bifidobacterium longum strain
Hartke, A., Benachour, A., Boutibonnes, P., & Auffray, Y. (1996) · Applied Microbiology and Biotechnology · doi:10.1007/s002530050660 · Cited by 9
DNA methyltransferases from Neisseria meningitidis and Neisseria gonorrhoeae FA1090 associated with mismatch nicking endonucleases
Kwiatek, A., Kobes, M., Olejnik, K., & Piekarowicz, A. (2004) · Microbiology · doi:10.1099/mic.0.27011-0 · Cited by 9
“The most common DNA MTases are associated with a cognate restriction endonuclease ( Wilson & Murray, 1991 ).”
Background
Photolabeling of the EcoP15 DNA methyltransferase with
Ahmad, I., & Rao, D. N. (1994) · Gene · doi:10.1016/0378-1119(94)90356-5 · Cited by 9
Organization and sequence of the SalI restriction-modification system
Rodicio, M. R., Quinton-Jager, T., Moran, L. S., Slatko, B. E., & Wilson, G. G. (1994) · Gene · doi:10.1016/0378-1119(94)90650-5 · Cited by 9
“(c) Comparison with other R-M systems The gene organization of the Sal1 system is similar to many type-II R-M systems, including AccI, BanI, BsuFI, D&I, EcoRI, HgiCI and DI, HindIII, HpuI, MwoI, NulIII, NgoPII, Sau3A1, SmaI and XbuI (Wilson and Murray, 1991).”
ResultSelf-citation
Theoretical model of restriction endonuclease HpaI in complex with DNA, predicted by fold recognition and validated by site‐directed mutagenesis
Skowronek, K. J., Kosiński, J., & Bujnicki, J. M. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20920 · Cited by 9
“among REases has lead to speculations that they may be products of convergent evolution.(7) Crystallographic analy-”
Background
Modulation of EcoKI restriction in vivo: role of the lambda Gam protein and plasmid metabolism
Salaj-Šmic, E., Maršić, N., Trgovčević, Ž., & Lloyd, R. G. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.6.1852-1856.1997 · Cited by 9
“, in foreign DNA), it acts as a restriction endonuclease (46, 47).”
Background
Mechanism of Action of Restriction Endonuclease EcoRV
Halford, S. E., Taylor, J. D., Vermote, C. L. M., & Vipond, I. B. (1993) · Nucleic acids and molecular biology · doi:10.1007/978-3-642-77950-3_4 · Cited by 9
Knowing Our Enemy in the Antimicrobial Resistance Era: Dissecting the Molecular Basis of Bacterial Defense Systems
Martínez, M., Rizzuto, I., & Molina, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094929 · Cited by 8
“Restriction–modification systems serve to distinguish self from non-self, cleaving phage-invading nucleic acids based on epigenetic modifications [44].”
Background
Concerted action at eight phosphodiester bonds by the BcgI restriction endonuclease
Marshall, J. J. T., Smith, R. M., Ganguly, S., & Halford, S. E. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr453 · Cited by 8
“Most restriction–modification (R–M) systems display two activities that act in response to a specific DNA sequence: a modification methyltransferase (MTase) that methylates a specific base within the sequence; and a restriction endonuclease (REase) that cleaves the DNA provided neither strand is modified (1).”
Background
Establishing genetic manipulation for novel strains of human gut bacteria
Sheridan, P. O., Al-Odat, M. A., & Scott, K. P. (2023) · Microbiome Research Reports · doi:10.20517/mrr.2022.13 · Cited by 8
Two different restriction-modification systems for degrading exogenous DNA in Paenibacillus polymyxa
Shen, M., Chen, Z., Mao, X., Wang, L., Liang, J., Huo, Q., Yin, X., Qiu, J., & Sun, D. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.09.016 · Cited by 8
Tetramerization at Low pH Licenses DNA Methylation Activity of M.HpyAXI in the Presence of Acid Stress
Narayanan, N., Banerjee, A. K., Jain, D., Kulkarni, D. S., Sharma, R., Nirwal, S., Rao, D. N., & Nair, D. T. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.001 · Cited by 8
Roles for Helicases as ATP-Dependent Molecular Switches
Szczelkun, M. D. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-5037-5_11 · Cited by 7
Plasmid pP62BP1 isolated from an Arctic Psychrobacter sp. strain carries two highly homologous type II restriction-modification systems and a putative organic sulfate metabolism operon
Lasek, R., Dziewit, Ł., & Bartosik, D. (2012) · Extremophiles · doi:10.1007/s00792-012-0435-2 · Cited by 8
“The aforementioned tail to tail organization of the ORFs of the pP62BP1 R-M1 and R-M2 systems with overlapping of their 30 ends is rather uncommon among the restrictionmodification systems (Wilson and Murray 1991).”
Background
Evolutionary change and phylogenetic relationships in light of horizontal gene transfer
Boto, L. (2015) · Journal of Biosciences · doi:10.1007/s12038-015-9514-8 · Cited by 9
“In bacteria, restriction/modification systems (Wilson and Murray 1991), the CRISPRs/Cas system (Horvath and J. Biosci.”
Composition and potential functions of the dominant microbiota in deep-sea hagfish gut from the South China Sea
Lian, C., Zhu, F.-C., Wei, Z., & He, L. (2021) · Deep Sea Research Part I Oceanographic Research Papers · doi:10.1016/j.dsr.2021.103488 · Cited by 8
Crystal structure of a putative DNA methylase TTHA0409 from Thermus thermophilus HB8
Morita, R., Ishikawa, H., Nakagawa, N., Kuramitsu, S., & Masui, R. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22158 · Cited by 8
The effect ofrecA mutation on the expression ofEcoKI andEcoR124Ihsd genes cloned in a multicopy plasmid
Hubáček, J., Holubová, I., & Weiserová, M. (1998) · Folia Microbiologica · doi:10.1007/bf02818573 · Cited by 8
Overexpression of BsoBI restriction endonuclease in E. coli, purification of the recombinant BsoBI, and identification of catalytic residues of BsoBI by random mutagenesis
Ruan, H., Lunnen, K. D., Pelletier, J. J., & Xu, S.-Y. (1997) · Gene · doi:10.1016/s0378-1119(96)00773-1 · Cited by 8

Authors: Wilson, G. G., & Murray, N. E.
Affiliations: New England Biolabs (United States) (US)
Venue: Annual Review of Genetics
Publisher: Annual Reviews
Published: 1991-12
Volume: 25
Issue: 1
Pages: 585-627
ISSN: 0066-4197 (ISSN-L)
1545-2948
DOI: 10.1146/annurev.ge.25.120191.003101
OpenAlex: W2179631201
Cited by: 714
References: 94
Citations by year: 2026: 11 · 2025: 13 · 2024: 14 · 2023: 22 · 2022: 15 · 2021: 13 · 2020: 18 · 2019: 20 · 2018: 18 · 2017: 14 · 2016: 22 · 2015: 18 · 2014: 30 · 2013: 22 · 2012: 33
FWCI: 9.78
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Genetics (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Chromosomal and Genetic Variations
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genome Rearrangement Algorithms
Keywords: restriction-modification systems, restriction enzymes, DNA methylation, DNA methyltransferases, bacterial defense against foreign DNA, gene duplication, homologous genes, orthology, paralogy
MeSH terms: Cloning, Molecular, DNA, Bacterial, DNA, Viral, Genes, Bacterial, Methylation, Terminology as Topic, Substrate Specificity, DNA Restriction-Modification Enzymes, Gene Expression Regulation, Bacterial

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