WhiB2/Rv3260c, a cell division-associated protein of Mycobacterium tuberculosis H37Rv, has properties of a chaperone

FEBS Journal

Volumn 279, Issue 15, 2012, Pages 2781-2792

  Konar, Monica ^a   Alam, Md Suhail ^a   Arora, Chandni ^a   Agrawal, Pushpa ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

Author keywords

chaperone; intramolecular disulfide bonds; Mycobacterium tuberculosis; WhiB2

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; CITRATE SYNTHASE; CYSTEINE; LUCIFERASE; PROTEIN WHIB2; THIOSULFATE SULFURTRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CELL DIVISION; CONTROLLED STUDY; DISULFIDE BOND; ENZYME REPRESSION; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN REFOLDING;

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; BASE SEQUENCE; CELL DIVISION; CHEMICAL PRECIPITATION; CITRATE (SI)-SYNTHASE; CYSTEINE; DNA, BACTERIAL; GENES, BACTERIAL; INSULIN; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; MYCOBACTERIUM TUBERCULOSIS; OXIDATION-REDUCTION; PROTEIN DENATURATION; SERINE;

ACTINOBACTERIA (CLASS); CORYNEBACTERINEAE; MYCOBACTERIUM TUBERCULOSIS; STREPTOMYCES;

EID: 84863849311     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08662.x     Document Type: Article

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