The non-canonical protein binding site at the monomer-monomer interface of yeast proliferating cell nuclear antigen (PCNA) regulates the Rev1-PCNA interaction and Polζ/Rev1-dependent translesion DNA synthesis

Journal of Biological Chemistry

Volumn 286, Issue 38, 2011, Pages 33557-33566

  Sharma, Neeru M ^a,b   Kochenova, Olga V ^a   Shcherbakova, Polina V ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b NEBRASKA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY BEADS; AMINO ACID SUBSTITUTION; DNA DAMAGES; DNA POLYMERASE; DNA REPAIR; GEL-FILTRATION CHROMATOGRAPHY; GENETIC ANALYSIS; GST PULL-DOWN; HYDROPHOBIC MOTIFS; INTER-DOMAIN; INTERMOLECULAR INTERFACES; MONOMER-MONOMER INTERFACES; NUCLEAR DNA; PHYSICAL INTERACTIONS; PRIMER TERMINUS; PROLIFERATING CELL NUCLEAR ANTIGENS; PROTEIN-BINDING SITES; REPLICATION FORK; TRANSLESION DNA SYNTHESIS; TRANSLESION SYNTHESIS;

AMINO ACIDS; ANTIGENS; BIOCHEMISTRY; CELL PROLIFERATION; DNA; GEL PERMEATION CHROMATOGRAPHY; POLYMERS; PROTEINS; SEEBECK EFFECT; YEAST;

MONOMERS;

CYCLINE; DNA POLYMERASE; DNA POLYMERASE REV1; DNA POLYMERASE SIGMA; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONTROLLED STUDY; DNA SYNTHESIS; FUNGAL STRAIN; GEL FILTRATION CHROMATOGRAPHY; GENE MUTATION; GENE REPLICATION; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS;

ANTIGENS, NUCLEAR; BINDING SITES; CATALYTIC DOMAIN; DNA DAMAGE; DNA REPAIR; DNA, FUNGAL; DNA-DIRECTED DNA POLYMERASE; MICROBIAL VIABILITY; MODELS, MOLECULAR; MUTANT PROTEINS; MUTATION; NUCLEOTIDYLTRANSFERASES; PROLIFERATING CELL NUCLEAR ANTIGEN; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; ULTRAVIOLET RAYS;

EID: 80053044268     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.206680     Document Type: Article

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