Initiation of translocation by Type I restriction-modification enzymes is associated with a short DNA extrusion [PDF]
Nucleic Acids Research, 2004 Recognition of 'foreign' DNA by Type I restriction-modification (R-M) enzymes elicits an ATP-dependent switch from methylase to endonuclease activity, which involves DNA translocation by the restriction subunit HsdR. Type I R-M enzymes are composed of three (Hsd) subunits with a stoichiometry of HsdR2:HsdM2:HsdS1 (R2-complex). However, the EcoR124I R-M
John van Noort +4 more
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Isolation of five type IIG restriction modification (RM) enzyme genes with different DNA recognition sites from a single environmental DNA sample [PDF]
African Journal of Biotechnology, 2019 A new method of screening type IIG restriction modification (RM) enzyme has been developed using REBASE, a database of all known and putative restriction enzymes and methyltransferases found throughout the bacterial genome sequences available in GENBANK.
Thi Kim Tuyen Le +2 more
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DNA-mediated coupling of ATPase, translocase and nuclease activities of a Type ISP restriction-modification enzyme [PDF]
Nucleic Acids Research, 2020 Abstract Enzymes involved in nucleic acid transactions often have a helicase-like ATPase coordinating and driving their functional activities, but our understanding of the mechanistic details of their coordination is limited. For example, DNA cleavage by the antiphage defense system Type ISP restriction-modification enzyme requires ...
Mahesh Kumar Chand +3 more
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Crystal structure of DNA sequence specificity subunit of a type I restriction-modification enzyme and its functional implications [PDF]
Proceedings of the National Academy of Sciences, 2005 Type I restriction-modification enzymes are differentiated from type II and type III enzymes by their recognition of two specific dsDNA sequences separated by a given spacer and cleaving DNA randomly away from the recognition sites. They are oligomeric proteins formed by three subunits: a specificity subunit, a methylation subunit, and a ...
Jeong‐Sun Kim +6 more
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Recycling of protein subunits during DNA translocation and cleavage by Type I restriction-modification enzymes [PDF]
Nucleic Acids Research, 2011 The Type I restriction-modification enzymes comprise three protein subunits; HsdS and HsdM that form a methyltransferase (MTase) and HsdR that associates with the MTase and catalyses Adenosine-5'-triphosphate (ATP)-dependent DNA translocation and cleavage. Here, we examine whether the MTase and HsdR components can 'turnover' in vitro, i.e. whether they
Michelle Simons, Mark D. Szczelkun
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Dissociation from DNA of Type III Restriction–Modification enzymes during helicase-dependent motion and following endonuclease activity [PDF]
Nucleic Acids Research, 2012 DNA cleavage by the Type III Restriction-Modification (RM) enzymes requires the binding of a pair of RM enzymes at two distant, inversely orientated recognition sequences followed by helicase-catalysed ATP hydrolysis and long-range communication. Here we addressed the dissociation from DNA of these enzymes at two stages: during long-range communication
Julia I. Toth +3 more
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Interaction between EcoRII restriction/modification enzymes and synthetic DNA fragments. Synthesis of substrates containing a single recognition site [PDF]
Biopolymers and Cell, 1987 Светлана А. Кузнецова +7 more
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Mapping DNA cleavage by the Type ISP restriction-modification enzymes following long-range communication between DNA sites in different orientations [PDF]
Nucleic Acids Research, 2015 The prokaryotic Type ISP restriction-modification enzymes are single-chain proteins comprising an Mrr-family nuclease, a superfamily 2 helicase-like ATPase, a coupler domain, a methyltransferase, and a DNA-recognition domain. Upon recognising an unmodified DNA target site, the helicase-like domain hydrolyzes ATP to cause site release (remodeling ...
Kara van Aelst +2 more
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Nucleic Acids ResearchAbstract We have determined multiple cryogenic electron microscopy (cryo-EM) structures of the Type IIB restriction–modification enzyme BsaXI. Such enzymes cleave DNA on both sides of their recognition sequence and share features of Types I, II, and III restriction systems.
Betty Shen +4 more
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PLOS Biology, 2016 [This corrects the article DOI: 10.1371/journal.pbio.1002442.].
The PLOS Biology Staff
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