Site-specific inhibition ofEcoRI restriction/modification enzymes by a DNA triple helix [PDF]
Nucleic Acids Research, 1990 The ability of oligopyrimidines to inhibit, through triple helix formation, the specific protein-DNA interactions of the EcoRI restriction and modification enzymes (EcoRI and MEcoRI) with their recognition sequence (GAATTC) was studied. The oligonucleotides (CTT)4 and (CTT)8 formed triplexes in plasmids at (GAA)n repeats containing EcoRI sites ...
Jeffery C. Hanvey +2 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,
Jeong‐Sun Kim +6 more
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Substrate DNA and cofactor regulate the activities of a multi-functional restriction-modification enzyme, BcgI [PDF]
Nucleic Acids Research, 1997 The BcgI restriction-modification system consists of two subunits, A and B. It is a bifunctional protein complex which can cleave or methylate DNA. The regulation of these competing activities is determined by the DNA substrates and cofactors. BcgI is an active endonuclease and a poor methyltransferase on unmodified DNA substrates. In contrast, BcgI is
Hyun-Hee Kong, Cassandra L. Smith
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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
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DNA cleavage and methylation specificity of the single polypeptide restriction–modification enzyme LlaGI [PDF]
Nucleic Acids Research, 2009 LlaGI is a single polypeptide restriction-modification enzyme encoded on the naturally-occurring plasmid pEW104 isolated from Lactococcus lactis ssp. cremoris W10. Bioinformatics analysis suggests that the enzyme contains domains characteristic of an mrr endonuclease, a superfamily 2 DNA helicase and a gamma-family adenine methyltransferase.
Rachel M. Smith +4 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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Historical Aspects of Restriction Endonucleases as Intelligent Scissors for Genetic Engineering
Fermentation, 2023 Restriction endonucleases are a component of restriction–modification systems, where the main biological function is to protect bacterial cells from incoming foreign DNA molecules.
Irina V. Alekseeva, Nikita A. Kuznetsov
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Recombination of constant and variable modules alters DNA sequence recognition by type IC restriction-modification enzymes. [PDF]
The EMBO Journal, 1992 EcoR124 and EcoDXXI are allelic type I restriction-modification (R-M) systems whose specificity genes consist of common structural elements: two variable regions are separated by a constant, homologous region containing a number of repetitive sequence elements. In vitro recombination of variable and constant elements has led to fully active, hybrid R-M
Marcel Gubler +4 more
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The Type ISP Restriction-Modification enzymes LlaBIII and LlaGI use a translocation-collision mechanism to cleave non-specific DNA distant from their recognition sites [PDF]
Nucleic Acids Research, 2012 The Type ISP Restriction-Modification (RM) enzyme LlaBIII is encoded on plasmid pJW566 and can protect Lactococcus lactis strains against bacteriophage infections in milk fermentations. It is a single polypeptide RM enzyme comprising Mrr endonuclease, DNA helicase, adenine methyltransferase and target-recognition domains. LlaBIII shares >95% amino acid
Eva Šišáková +3 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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