Three residues of the interdomain linker determine the conformation and single-base deletion fidelity of y-family translesion polymerases

Journal of Biological Chemistry

Volumn 289, Issue 10, 2014, Pages 6323-6331

  Mukherjee, Purba ^a   Wilson, Ryan C ^a   Lahiri, Indrajit ^a   Pata, Janice D ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

ACTIVE SITE; INCORPORATION RATES; INTER-DOMAIN; LESION BYPASS; TRANSLESION; TRANSLESION SYNTHESIS;

POLYMERS;

AMINO ACID; DNA POLYMERASE; PROTEIN DBH; PROTEIN DPO4; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; DNA SYNTHESIS; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME SUBSTRATE; GENE DELETION; INTERDOMAIN LINKER; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE ALIGNMENT; SINGLE BASE DELETION;

DNA POLYMERASE; DNA REPLICATION; ENZYME MUTATION; FIDELITY; KINETICS; PROTEIN CONFORMATION; STRUCTURAL BIOLOGY; TRANSLESION SYNTHESIS; Y-FAMILY POLYMERASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARCHAEAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DNA POLYMERASE BETA; DNA REPLICATION; DNA-DIRECTED DNA POLYMERASE; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SEQUENCE DELETION; SULFOLOBUS;

EID: 84896795806     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.537860     Document Type: Article

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