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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Meselson, M. S., & Yuan, R. T. (1968) · Nature · doi:10.1038/2171110a0 · Cited by 819
Group I introns as mobile genetic elements: Facts and mechanistic speculations — a review
Dujon, B. (1989) · Gene · doi:10.1016/0378-1119(89)90034-6 · Cited by 478
Restriction Endonucleases in the Analysis and Restructuring of DNA Molecules
Nathans, D., & Smith, H. O. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.001421 · Cited by 467
Substrate and sequence specificity of a eukaryotic DNA methylase
Gruenbaum, Y., Cedar, H., & Razin, A. (1982) · Nature · doi:10.1038/295620a0 · Cited by 436
DNA Nucleotide Sequence Restricted by the RI Endonuclease
Hedgpeth, J., Goodman, H. M., & Boyer, H. W. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.11.3448 · Cited by 363
McrA and McrB restriction phenotypes of someE.colistrains and implications for gene cloning
Raleigh, E. A., Murray, N. E., Revel, H. R. B., Blumenthal, R., Westaway, D. A., Reith, A. D., Rigby, P. W. J., Elhai, J., & Hanahan, D. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.4.1563 · Cited by 342
Self-citation
DNA Restriction and Modification Mechanisms in Bacteria
Boyer, H. W. (1971) · Annual Review of Microbiology · doi:10.1146/annurev.mi.25.100171.001101 · Cited by 330
Restriction and Modification of DNA
Meselson, M. S., Yuan, R., & Heywood, J. (1972) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.41.070172.002311 · Cited by 290
The construction in vitro of transducing derivatives of phage lambda
Borck, J. (1976) · Medical Entomology and Zoology · Cited by 259
The great GATC: DNA methylation in E. coli
Barras, F., & Marinus, M. G. (1989) · Trends in Genetics · doi:10.1016/0168-9525(89)90054-1 · Cited by 209

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“(Bickle and Kriiger 1993; Wilson and Murray 1991).”
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Uyen, N. T., Nishi, K., Park, S.-Y., Choi, J.-W., Lee, H.-J., & Kim, J. (2008) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309108027516 · Cited by 2
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Background
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Background
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“Molecular Biology Reports 2012; 39(5): 5607.”
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Neve, H., & Josephsen, J. (2004) · CRC Press eBooks · doi:10.1201/9780824752033.ch8 · Cited by 2
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“Enzymes with 22–34% sequence identity sometimes encode REases with altered target sites (Wilson and Murray, 1991; Pingoud et al., 2014).”
BackgroundMethod
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Ruan, H., Lunnen, K. D., Scott, M. E., Moran, L. S., Slatko, B. E., Pelletier, J. J., Hess, E. J., Benner, J., Wilson, G. G., & Xu, S.-Y. (1996) · Molecular and General Genetics MGG · doi:10.1007/bf02173975 · Cited by 2
“However, methylases that modify N6 adenine, C5 cytosine, or N4 cytosine contain sequence similarities/conserved motifs within each modification family (Heitman 1993; Noyer-Weidner and Trautner 1993; Posfai et al. 1989; Roberts and Halford 1993; Wilson and Murray 1991).”
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Background
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“nosyl-L-methionine (AdoMet, methyl donor) binding (motifs X-I-II-III), catalytic function (motifs IV-V-VIVII-VIII), and DNA target recognizing (TRD) [9,2].”
BackgroundInfluential
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Background
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Background
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Background
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Saavedra, C. P., Vásquez, C. C., & Encinas, M. V. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00453.x · Cited by 1
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Vanamee, É. S., & Aggarwal, A. K. (2004) · Handbook of Metalloproteins · doi:10.1002/0470028637.met063 · Cited by 1
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Wijenayake, S. (2012) · doi:10.22215/etd/2012-07415 · Cited by 1
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Hyun, S., & Park, P. (2010) · InTech eBooks · doi:10.5772/7218
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Moreira, L. M. (2006) · doi:10.11606/t.46.2006.tde-20042007-160036
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Adib, M., Sarker, M. M. H., Ahmed, S. S., Ariwa, E. I., & Siddiqui, F. A. (2010) · Communications in computer and information science · doi:10.1007/978-3-642-14306-9_4
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Background
Global analysis of the methyl-CpG binding protein MeCP2
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Background
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Tao, W., Li, W., & Yu, Z. (2009) · Molecular Biology · doi:10.1134/s0026893309030182
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Waleron, K., Waleron, M., Osipiuk, J., Podhajska, A. J., & Łojkowska, E. (2006) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2005.02766.x
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Background
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Andres, S. (2010) · Figshare
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Yan, C. (2005) · doi:10.31274/rtd-180813-2240
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Self-citation
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Cao, B., Chen, C., DeMott, M. S., Cheng, Q., Clark, T. A., Xiong, X., Zheng, X., Butty, V. L., Levine, S. S., Yuan, G., et al. (2013) · RePEc: Research Papers in Economics
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Singh, S., & Guruprasad, L. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b08433
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Background
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Jurkowski, T. P. (2009)
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Background
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“Additionally, it is generally known that most bacteria have restriction modification (RM) systems that prevent the entry of foreign DNA into the host cell (Wilson and Murray, 1991).”
Background
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Bibliography
(1997) · Elsevier eBooks · doi:10.1016/b978-012323445-2/50024-9
Stammdesign in B. licheniformis
Rachinger, M. (2010) · doi:10.53846/goediss-375
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“Enzymes with 22% to 34% sequence identity sometimes encode REases with altered target sites ([7; 30].”
BackgroundMethod
References
(2004) · Wiley eBooks · doi:10.1002/0471647527.refs
Moonlighting and Mimicry: Identification and Functional Characterization of a SAM-dependent Methyltransferase Responsible for Methylation of EF-Tu in Pseudomonas Aeruginosa
Owings, J. P. (2014) · doi:10.18130/v30r8x
Megváltoztatott szekvenciaspecifitású DNS metiltranszferázok létrehozása és vizsgálata
Tímár, E. (2017) · doi:10.14232/phd.3132
Cloning
Wilson, D. B. (2002) · Wiley Encyclopedia of Molecular Medicine · doi:10.1002/0471203076.emm0705
Cloning
Wilson, D. B. (2002) · Encyclopedia of Molecular Biology · doi:10.1002/047120918x.emb0273
Characterization of the Subunits of the McrBC Restriction System in Escherichia Coli K12.
Beary, T. P. (1993) · doi:10.31390/gradschool_disstheses.5485
Purification, Crystallization, and Preliminary X-Ray Analysis of the BseCI DNA Methyltransferase from Geobacillus stearothermophilus in Complex with Its Cognate DNA in Two Distinct Methylation States
Kouyianou, K., Mitsikas, D. A., Kotsifaki, D., Providaki, M., Bouriotis, V., & Kokkinidis, M. (2022) · Crystallography Reports · doi:10.1134/s1063774522070070
Engineering of the temperate Burkholderia phage Milagro for use as a therapeuticPreprint
Yao, G. W., Le, T., Korn, A. M., Peterson, H., Liu, M., Gonzalez, C., & Gill, J. J. (2023) · Research Square · doi:10.21203/rs.3.rs-2626327/v1
Approaches for introducing large DNA molecules into bacterial cells
Nishida, H. (2023) · Journal of Applied Microbiology · doi:10.1093/jambio/lxad059
Genome diversity of Alteromonas macleodii isolated from the Persian Gulf and the Atlantic Ocean
Varasteh, T., Ahmadi, R. A., Mendonça, B., Santos, E. D. O., Shokri, M. R., Tschoeke, D. A., Thompson, C. C., & Thompson, F. L. (2025) · Regional Studies in Marine Science · doi:10.1016/j.rsma.2025.104140
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Belizário, J. E., Occhiucci, J. M., Garay-Malpartida, M., & Silva, J. (2025) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2025.07.003
A single molecule nanoactuator: toward a device for drug discovery at the limits of sensitivity
Youell, J., & Firman, K. (2010)
Additional file 5 of A coarse-graining, ultrametric approach to resolve the phylogeny of prokaryotic strains with frequent homologous recombination
Pang, T. Y. (2020) · Figshare · doi:10.6084/m9.figshare.12270482

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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