The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-double-stranded DNA junction

Journal of Biological Chemistry

Volumn 283, Issue 3, 2008, Pages 1732-1743

  Pugh, Robert A ^a   Honda, Masayoshi ^a   Leesley, Haley ^a   Thomas, Alvin ^a   Lin, Yuyen ^a   Nilges, Mark J ^a   Cann, Isaac K O ^a   Spies, Maria ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; DNA; HYDROLYSIS; MOLECULAR INTERACTIONS; MUTAGENESIS;

DNA REPAIR; HELICASE ACTIVITY; PHENOTYPES;

ENZYME ACTIVITY;

ADENOSINE TRIPHOSPHATE; CHECKPOINT KINASE RAD3; DNA; DOUBLE STRANDED DNA; FLUORESCENT DYE; HELICASE; IRON; IRON SULFUR PROTEIN; SINGLE STRANDED DNA;

ARTICLE; DNA STRAND; ENZYME BINDING; ENZYME SPECIFICITY; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; ARCHAEA; ARCHAEAL PROTEINS; BIOLOGICAL TRANSPORT; DNA HELICASES; DNA REPLICATION; DNA, CRUCIFORM; DNA, SINGLE-STRANDED; HYDROLYSIS; IRON-SULFUR PROTEINS; LIGANDS; MUTANT PROTEINS; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

ARCHAEA; FERROPLASMA ACIDARMANUS;

EID: 38349091095     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M707064200     Document Type: Article

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