Uracil DNA glycosylase activity on nucleosomal DNA depends on rotational orientation of targets

Journal of Biological Chemistry

Volumn 285, Issue 4, 2010, Pages 2876-2885

  Cole, Hope A ^a,b   Tabor Godwin, Jenna M ^a,c   Hayes, Jeffrey J ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

^b EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^c SAN DIEGO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL PROCESS; GLOBULAR DOMAINS; HISTONE OCTAMERS; HISTONE-DNA INTERACTIONS; HOT SPOT; LINKER HISTONES; NAKED DNA; NUCLEOSOME CORE; NUCLEOSOMES; ROTATIONAL ORIENTATION; SPECIFIC LOCATION; URACIL-DNA GLYCOSYLASE;

GENES; PROTEINS;

DNA;

DNA; THYMIDINE; URACIL DNA GLYCOSIDASE; BACTERIAL DNA; ESCHERICHIA COLI PROTEIN; HISTONE;

ARTICLE; ENZYME ACTIVITY; GEL ELECTROPHORESIS; GENE DISRUPTION; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN PROCESSING; CHEMISTRY; CHROMATIN; DNA REPAIR; ENZYME ACTIVATION; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; METABOLISM; PHYSIOLOGY; STEREOISOMERISM;

CHROMATIN; DNA REPAIR; DNA, BACTERIAL; ENZYME ACTIVATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HISTONES; NUCLEOSOMES; STEREOISOMERISM; SUBSTRATE SPECIFICITY; URACIL-DNA GLYCOSIDASE;

EID: 77449137042     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.073544     Document Type: Article

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