Single molecule analysis of a red fluorescent RecA protein reveals a defect in nucleoprotein filament nucleation that relates to its reduced biological functions

Journal of Biological Chemistry

Volumn 284, Issue 28, 2009, Pages 18664-18673

  Handa, Naofumi ^a,b   Amitani, Ichiro ^a   Gumlaw, Nathan ^c   Sandler, Steven J ^c   Kowalczykowski, Stephen C ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF TOKYO   (Japan)

^c UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATP-ASE ACTIVITY; BIOLOGICAL FUNCTIONS; DNA STRANDS; DOUBLE STRANDED DNA; DUPLEX DNA; FILAMENT ASSEMBLY; FUNCTIONAL PROTEINS; FUSION PROTEINS; IN-SITU; IN-VITRO; IN-VITRO ANALYSIS; IN-VIVO; NUCLEOPROTEIN FILAMENTS; PROTEIN BEHAVIOR; PROTEIN LOCALIZATION; RECA PROTEINS; RED FLUORESCENT PROTEINS; REDUCED FREQUENCY; SINGLE MOLECULE; SINGLE MOLECULE LEVEL; SINGLE-MOLECULE ANALYSIS; SINGLE-STRANDED DNA; SINGLE-STRANDED DNA-BINDING PROTEINS; WILD-TYPE PROTEINS;

FILAMENTS (LAMP); FLUORESCENCE; GENES; MOLECULES; NUCLEATION; NUCLEIC ACIDS; PROTEINS;

DNA;

ADENOSINE TRIPHOSPHATASE; DOUBLE STRANDED DNA; NUCLEOPROTEIN; RECA PROTEIN; RED FLUORESCENT PROTEIN; SINGLE STRANDED DNA BINDING PROTEIN;

ARTICLE; BIOLOGICAL ACTIVITY; CONTROLLED STUDY; DNA RECOMBINATION; DNA STRUCTURE; ENZYME ACTIVITY; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE;

CELL NUCLEUS; DNA; DNA, SINGLE-STRANDED; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; LUMINESCENT PROTEINS; NUCLEOPROTEINS; PLASMIDS; PROTEIN BINDING; REC A RECOMBINASES; RECOMBINATION, GENETIC; SENSITIVITY AND SPECIFICITY; ULTRAVIOLET RAYS;

EID: 67650567353     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.004895     Document Type: Article

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