Mycobacterium smegmatis RecA protein is structurally similar to but functionally distinct from Mycobacterium tuberculosis RecA

Proteins: Structure, Function and Genetics

Volumn 53, Issue 1, 2003, Pages 6-17

  Ganesh, N ^a   Muniyappa, K ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

D loops; Joint molecules; Mycobacteria; RecA; Recombination; SSB

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTIPORTER; RECA PROTEIN; SINGLE STRANDED DNA BINDING PROTEIN; SODIUM CHLORIDE;

ARTICLE; CATALYSIS; DNA PROTEIN COMPLEX; DNA STRAND; ESCHERICHIA COLI; GEL MOBILITY SHIFT ASSAY; HYDROLYSIS; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; DNA, SINGLE-STRANDED; DNA-BINDING PROTEINS; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; REC A RECOMBINASES; RECOMBINATION, GENETIC; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM CHLORIDE; SPECIES SPECIFICITY;

BACTERIA (MICROORGANISMS); CORYNEBACTERINEAE; ESCHERICHIA COLI; MYCOBACTERIUM; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

EID: 0041819759     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10433     Document Type: Article

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