Mycobacterium smegmatis RqlH defines a novel clade of bacterial RecQ-like DNA helicases with ATP-dependent 3′-5′ translocase and duplex unwinding activities

Nucleic Acids Research

Volumn 40, Issue 10, 2012, Pages 4604-4614

  Ordonez, Heather ^a   Unciuleac, Mihaela ^a   Shuman, Stewart ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DOUBLE STRANDED DNA; HELICASE; PROTEIN RQIH; RECQ HELICASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; BACTERIUM IDENTIFICATION; CARBOXY TERMINAL SEQUENCE; CLADISTICS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME LOCALIZATION; ENZYME STRUCTURE; ESCHERICHIA COLI; GENETIC CODE; MYCOBACTERIUM SMEGMATIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN TRANSPORT; SPECIES COMPARISON; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DNA; DNA, SINGLE-STRANDED; KINETICS; METALS; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM SMEGMATIS; PHYLOGENY; PROTEIN STRUCTURE, TERTIARY; RECQ HELICASES; SUBSTRATE SPECIFICITY;

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

EID: 84861556085     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks046     Document Type: Article

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