A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo

Journal of Biological Chemistry

Volumn 272, Issue 1, 1997, Pages 572-579

  Brosh Jr , Robert M ^a   Matson, Steven W ^a  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; DOUBLE STRANDED DNA; HELICASE; MUTANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; DNA DAMAGE; ENZYME SUBSTRATE; ESCHERICHIA COLI; EXCISION REPAIR; GENETIC COMPLEMENTATION; NONHUMAN; PHENOTYPE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; ULTRAVIOLET IRRADIATION;

ADENOSINE TRIPHOSPHATASES; BACTERIAL PROTEINS; DNA HELICASES; DNA REPAIR; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; ULTRAVIOLET RAYS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; PROKARYOTA;

EID: 15444357274     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.1.572     Document Type: Article

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