Oxidation of a single active site suffices for the functional inactivation of the dimeric Bacillus subtilis OhrR repressor in vitro

Nucleic Acids Research

Volumn 37, Issue 4, 2009, Pages 1174-1181

  Eiamphungporn, Warawan ^a   Soonsanga, Sumarin ^a   Lee, Jin Won ^b   Helmann, John D ^a  

^a Department of Molecular Biology and Genetics   (United States)

^b Hanyang University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; MONOMER; PROTEIN OHRR; REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS SUBTILIS; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DNA BINDING; ENZYME ACTIVE SITE; GENE LOCUS; HUMAN; IN VITRO STUDY; MUTATIONAL ANALYSIS; OXIDATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; WILD TYPE;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; BENZENE DERIVATIVES; CYSTEINE; LINOLEIC ACIDS; LIPID PEROXIDES; MUTATION; OXIDANTS; OXIDATION-REDUCTION; PEROXIDES; REPRESSOR PROTEINS; RNA, MESSENGER;

BACILLUS SUBTILIS;

EID: 62549099131     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkn1052     Document Type: Article

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