N-terminal truncations in the FhlA protein result in formate- and MoeA-independent expression of the hyc (formate hydrogenlyase operon of Escherichia coli

Microbiology

Volumn 147, Issue 11, 2001, Pages 3093-3104

  Self, W T ^a   Hasona, A ^a   Shanmugam, K T ^a  

^a UNIVERSITY OF FLORIDA   (United States)

Author keywords

FhlA mutations; Molybdenum; Operon regulation

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; AMINO ACID; BACTERIAL DNA; BETA GALACTOSIDASE; CARBON DIOXIDE; CARRIER PROTEIN; FORMATE DEHYDROGENASE; FORMIC ACID; HYDROGEN; HYDROGENASE; MOLYBDIC ACID;

AMINO ACID DEFICIENCY; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CYTOPLASM; DNA BINDING; DNA PROTEIN COMPLEX; ELECTRON; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME MECHANISM; ESCHERICHIA COLI; GENE ACTIVATION; GENE DELETION; GENE MUTATION; GENETIC ANALYSIS; GENETIC TRANSCRIPTION; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; OPERON; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN INTERACTION; PROTEIN MOTIF; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURAL GENE; TRANSCRIPTION REGULATION;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0035168344     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-147-11-3093     Document Type: Article

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