Results 11 to 20 of about 185,882 (314)

DNA cleavage and methylation specificity of the single polypeptide restriction–modification enzyme LlaGI [PDF]

open access: goldNucleic 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
openalex   +4 more sources

Substrate DNA and cofactor regulate the activities of a multi-functional restriction-modification enzyme, BcgI [PDF]

open access: bronzeNucleic 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
openalex   +4 more sources

DNA duplexes with reactive dialdehyde groups as novel reagents for cross-linking to restriction- modification enzymes [PDF]

open access: bronzeNucleic Acids Research, 1997
To create new, effective reagents for affinity modification of restriction-modification (R-M) enzymes, a regioselective method for reactive dialdehyde group incorporation into oligonucleotides, based on insertion of a 1-beta-D-galactopyranosylthymine residue, has been developed. We synthesized DNA duplex analogs of the substrates of the Eco RII and Mva
Maxim G. Brevnov   +8 more
openalex   +4 more sources

Site-specific inhibition ofEcoRI restriction/modification enzymes by a DNA triple helix [PDF]

open access: bronzeNucleic 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
openalex   +4 more sources

Recombination of constant and variable modules alters DNA sequence recognition by type IC restriction-modification enzymes. [PDF]

open access: bronzeThe 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
openalex   +3 more sources

The single polypeptide restriction–modification enzyme LlaGI is a self-contained molecular motor that translocates DNA loops [PDF]

open access: goldNucleic Acids Research, 2009
To cleave DNA, the single polypeptide restriction-modification enzyme LlaGI must communicate between a pair of indirectly repeated recognition sites. We demonstrate that this communication occurs by a 1-dimensional route, namely unidirectional dsDNA loop translocation rightward of the specific recognition sequence 5'-CTnGAyG-3' as written (where n is ...
Rachel M. Smith   +2 more
openalex   +4 more sources

DNA cleavage by Type ISP Restriction–Modification enzymes is initially targeted to the 3′-5′ strand [PDF]

open access: goldNucleic Acids Research, 2012
The mechanism by which a double-stranded DNA break is produced following collision of two translocating Type I Restriction-Modification enzymes is not fully understood. Here, we demonstrate that the related Type ISP Restriction-Modification enzymes LlaGI and LlaBIII can cooperate to cleave DNA following convergent translocation and collision.
Kara van Aelst   +2 more
openalex   +4 more sources

A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes [PDF]

open access: goldNucleic Acids Research, 2018
Restriction Modification (RM) systems prevent the invasion of foreign genetic material into bacterial cells by restriction and protect the host's genetic material by methylation. They are therefore important in maintaining the integrity of the host genome.
Edward Kenneth Merrick Bower   +6 more
openalex   +6 more sources

Cloning, crystallization and preliminary X-ray diffraction analysis of an intact DNA methyltransferase of a type I restriction–modification enzyme fromVibrio vulnificus [PDF]

open access: bronzeActa Crystallographica Section F Structural Biology Communications, 2014
Independently of the restriction (HsdR) subunit, the specificity (HsdS) and methylation (HsdM) subunits interact with each other, and function as a methyltransferase in type I restriction–modification systems. A single gene that combines the HsdS and HsdM subunits inVibrio vulnificusYJ016 was expressed and purified.
Thi Yen Ly Huynh   +2 more
openalex   +5 more sources

Time-resolved fluorescence of 2-aminopurine in DNA duplexes in the presence of the EcoP15I Type III restriction–modification enzyme

open access: hybridBiochemical and Biophysical Research Communications, 2014
EcoP15I is a Type III DNA restriction and modification enzyme of Escherichia coli. We show that it contains two modification (Mod) subunits for sequence-specific methylation of DNA and one copy of a restriction endonuclease (Res) subunit for cleavage of DNA containing unmethylated target sequences. Previously the Mod2 dimer in the presence of cofactors
Long Ma   +4 more
openalex   +4 more sources

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