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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
33
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pubmed:dateCreated |
1991-12-26
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pubmed:databankReference |
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pubmed:abstractText |
The fdnGHI operon of Escherichia coli encodes nitrate-inducible formate dehydrogenase. We report here the entire nucleotide sequence of fdnGHI. The sequence contains three open reading frames of sizes appropriate to encode the three subunits of formate dehydrogenase-N. fdnG contains an in-frame UGA codon that specifies selenocysteine incorporation, and the predicted amino acid sequence of FdnG shows similarity to two other bacterial formate dehydrogenase enzymes. FdnH contains 4 cysteine clusters typical of those found in iron-sulfur proteins. FdnG also contains a cysteine cluster. Evidence from sequence and spectral analyses suggest that FdnI encodes cytochrome bFdn556. Implications for the membrane topology of formate dehydrogenase-N and its mechanism of proton translocation are discussed.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Codon,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome b Group,
http://linkedlifedata.com/resource/pubmed/chemical/Formate Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrates,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Organoselenium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Selenocysteine,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome b556
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
266
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pubmed:geneSymbol |
fdnG,
fdnH,
fdnI
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
22380-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1834669-Amino Acid Sequence,
pubmed-meshheading:1834669-Base Sequence,
pubmed-meshheading:1834669-Cloning, Molecular,
pubmed-meshheading:1834669-Codon,
pubmed-meshheading:1834669-Cysteine,
pubmed-meshheading:1834669-Cytochrome b Group,
pubmed-meshheading:1834669-Enzyme Induction,
pubmed-meshheading:1834669-Escherichia coli,
pubmed-meshheading:1834669-Formate Dehydrogenases,
pubmed-meshheading:1834669-Gene Expression Regulation, Bacterial,
pubmed-meshheading:1834669-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:1834669-Genes, Bacterial,
pubmed-meshheading:1834669-Genotype,
pubmed-meshheading:1834669-Molecular Sequence Data,
pubmed-meshheading:1834669-Nitrates,
pubmed-meshheading:1834669-Oligodeoxyribonucleotides,
pubmed-meshheading:1834669-Open Reading Frames,
pubmed-meshheading:1834669-Operon,
pubmed-meshheading:1834669-Organoselenium Compounds,
pubmed-meshheading:1834669-Plasmids,
pubmed-meshheading:1834669-Recombinant Fusion Proteins,
pubmed-meshheading:1834669-Restriction Mapping,
pubmed-meshheading:1834669-Selenocysteine,
pubmed-meshheading:1834669-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1834669-beta-Galactosidase
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pubmed:year |
1991
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pubmed:articleTitle |
Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine.
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pubmed:affiliation |
Section of Microbiology, Cornell University, Ithaca, New York 14853-8101.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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