CLONING AND SEQUENCING OF A PUTATIVE ESCHERICHIA-COLI [NIFE] HYDROGENASE-1 OPERON CONTAINING 6 OPEN READING FRAMES

被引：125

作者：

MENON, NK ^{[1
]}

ROBBINS, J ^{[1
]}

PECK, HD ^{[1
]}

CHATELUS, CY ^{[1
]}

CHOI, ES ^{[1
]}

PRZYBYLA, AE ^{[1
]}

机构：

[1] UNIV GEORGIA,SCH CHEM SCI,DEPT BIOCHEM,ATHENS,GA 30602

来源：

JOURNAL OF BACTERIOLOGY | 1990年 / 172卷 / 04期

关键词：

D O I：

10.1128/jb.172.4.1969-1977.1990

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 NH2-terminal sequences of purified subunits (kindly provided by K. Francis and K.T. Shanmugam). The structural genes formed part of a putative operon that contained four additional open reading frames. We 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.

引用

页码：1969 / 1977

页数：9

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