Source:http://linkedlifedata.com/resource/pubmed/id/10627036
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
2000-2-17
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| pubmed:databankReference | |
| pubmed:abstractText |
We have conducted the genetic analysis of fermentative nitrate reduction in Clostridium perfringens, a strict anaerobic bacterium. Nitrate reductase (NarA) was purified from the cytoplasmic fraction of the organism. Using a degenerate primer designed from its N-terminal amino acid sequence, a 9.5 kb fragment containing seven ORFs was cloned. The molecular mass and N-terminal amino acid sequence predicted from the nucleotide sequence of ORF 4 coincided with those determined for the purified NarA, indicating that ORF 4 corresponds to a narA gene. ORFs 5 and 6 encode a 15.4 kDa ferredoxin-like protein containing four iron-sulfur clusters and a 45 kDa protein homologous to NADH oxidase, respectively. Analyses involving primer extension and Northern blotting revealed that these three ORFs are transcribed as a polycistronic message. The ORF 5- and ORF 6-encoded proteins were shown by immunoblotting to be synthesized by cells grown in the presence of nitrate. Thus, these two proteins are likely to function as electron-transfer components in nitrate reduction in C perfringens. The 9.5 kb fragment and a downstream region of 6.1 kb do not contain any genes involved in nitrate uptake or nitrite reduction. Instead, all 5 ORFs downstream of ORF 6 are homologous to genes reported for molybdopterin biosynthesis, unlike the genomic organization already determined for the respiratory and assimilatory nitrate-reduction systems. The evolutionary relationships between these two nitrate-reduction systems and the fermentative one based on the results of comparative genetic analysis are discussed.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ferredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/NADH oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrate Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrate Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrates,
http://linkedlifedata.com/resource/pubmed/chemical/Pterins,
http://linkedlifedata.com/resource/pubmed/chemical/molybdopterin guanine dinucleotide,
http://linkedlifedata.com/resource/pubmed/chemical/narA protein, Bacillus subtilis
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| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
1350-0872
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
145 ( Pt 12)
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3377-87
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10627036-Amino Acid Sequence,
pubmed-meshheading:10627036-Bacterial Proteins,
pubmed-meshheading:10627036-Cloning, Molecular,
pubmed-meshheading:10627036-Clostridium perfringens,
pubmed-meshheading:10627036-Ferredoxins,
pubmed-meshheading:10627036-Guanine Nucleotides,
pubmed-meshheading:10627036-Immunoblotting,
pubmed-meshheading:10627036-Molecular Sequence Data,
pubmed-meshheading:10627036-Multienzyme Complexes,
pubmed-meshheading:10627036-Multigene Family,
pubmed-meshheading:10627036-NADH, NADPH Oxidoreductases,
pubmed-meshheading:10627036-Nitrate Reductase,
pubmed-meshheading:10627036-Nitrate Reductases,
pubmed-meshheading:10627036-Nitrates,
pubmed-meshheading:10627036-Operon,
pubmed-meshheading:10627036-Oxidation-Reduction,
pubmed-meshheading:10627036-Pterins,
pubmed-meshheading:10627036-Sequence Analysis, DNA
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| pubmed:year |
1999
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| pubmed:articleTitle |
Analysis of genes involved in nitrate reduction in Clostridium perfringens.
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| pubmed:affiliation |
Department of Microbiology, Faculty of Medicine, Kagawa Medical University, Kita-gun, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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