Cloning and sequencing of a putative Escherichia coli (NiFe) hydrogenase-1 operon containing six open reading frames

Journal Article · Sun Apr 01 04:00:00 EDT 1990 · Journal of Bacteriology; (United States)

OSTI ID:5604959

Menon, N K; Robbins, J; Peck, Jr, H D; Chatelus, C Y; Choi, Euisung; Przybyla, ^[1]

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1. Univ. of Georgia, Athens (United States)

DNA encompassing the structural genes of an Escherichia coli (NiFe) hydrogenase has been cloned and sequenced. The genes were identified as those encoding the large and small subunits of hydrogenase isozyme 1 based on NH{sub 2}-terminal sequences of purified subunits. The structural genes formed part of a putative operon that contained four additional open reading frames. The authors have designated the operon hya and the six open reading frames hyaA through F. hyaA and hyaB encode the small and large structural subunits, respectively. The nucleotide-derived amino acid sequence of hyaC has a calculated molecular mass of 27.6 kilodaltons, contains 20% aromatic residues, and has four potential membrane-spanning regions. Open reading frames hyaD through F could encode polypeptides of 21.5, 14.9, and 31.5 kilodaltons, respectively. These putative peptides have no homology to other reported protein sequences, and their functions are unknown.

• OSTI ID: 5604959
• Journal Information: Journal of Bacteriology; (United States), Journal Name: Journal of Bacteriology; (United States) Vol. 172:4; ISSN JOBAA; ISSN 0021-9193
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
BACTERIA
CLONING
DNA
DNA SEQUENCING
ENZYMES
ESCHERICHIA COLI
GENE OPERONS
GENES
HYDROGENASES
MICROORGANISMS
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PEPTIDES
POLYPEPTIDES
PROTEINS
STRUCTURAL CHEMICAL ANALYSIS