ATP binding and hydrolysis by Saccharomyces cerevisiae Msh2-Msh3 are differentially modulated by mismatch and double-strand break repair DNA substrates

DNA Repair

Volumn 18, Issue 1, 2014, Pages 18-30

  Kumar, Charanya ^a   Eichmiller, Robin ^a   Wang, Bangchen ^a   Williams, Gregory M ^a   Bianco, Piero R ^b   Surtees, Jennifer A ^a  

^a UNIVERSITY AT BUFFALO   (United States)

^b UNIVERSITY AT BUFFALO   (United States)

Author keywords

3' non homologous tail removal; ATP binding hydrolysis; Double strand break repair; Mismatch repair; Msh2 Msh3

Indexed keywords

ADENOSINE TRIPHOSPHATE; HYDROLASE; PROTEIN MSH2; PROTEIN MSH3; DNA BINDING PROTEIN; FUNGAL DNA; MSH2 PROTEIN, S CEREVISIAE; MSH3 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; ATPASE ACTIVITY ASSAY; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; DNA BINDING; DNA REPAIR; DOUBLE STRANDED DNA BREAK; ENZYME SPECIFICITY; GEL MOBILITY SHIFT ASSAY; GENE DELETION; INDEL MUTATION; KINETICS; MISMATCH REPAIR; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN HYDROLYSIS; REGULATORY MECHANISM; SACCHAROMYCES CEREVISIAE; CHEMISTRY; ENZYME ACTIVE SITE; GENETICS; HYDROLYSIS; METABOLISM; MUTATION; PHENOTYPE;

SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATE; CATALYTIC DOMAIN; DNA BREAKS, DOUBLE-STRANDED; DNA MISMATCH REPAIR; DNA, FUNGAL; DNA-BINDING PROTEINS; HYDROLYSIS; KINETICS; MUTATION; MUTS HOMOLOG 2 PROTEIN; PHENOTYPE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY;

EID: 84900306397     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2014.03.032     Document Type: Article

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