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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
1999-3-5
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pubmed:databankReference | |
pubmed:abstractText |
Neelaredoxin, a small non-heme blue iron protein from the sulfate-reducing bacterium Desulfovibrio gigas [Chen, L., Sharma, P., LeGall, J., Mariano, A.M., Teixeira M. and Xavier, A.V. (1994) Eur. J. Biochem. 226, 613-618] is shown to be encoded by a polycistronic unit which contains two additional open reading frames (ORF-1 and ORF-2) coding for chemotaxis-like proteins. ORF-1 has domains highly homologous with those structurally and functionally important in methyl-accepting chemotaxis proteins, including two putative transmembrane helices, potential methylation sites and the interaction domain with CheW proteins. Interestingly, ORF-2 encodes a protein having homologies with CheW proteins. Neelaredoxin is also shown to have significant superoxide dismutase activity (1200 U. mg-1), making it a novel type of iron superoxide dismutase. Analysis of genomic data shows that neelaredoxin-like putative polypeptides are present in strict anaerobic archaea, suggesting that this is a primordial superoxide dismutase. The three proteins encoded in this operon may be involved in the oxygen-sensing mechanisms of this anaerobic bacterium, indicating a possible transcriptional mechanism to sense and respond to potential stress agents.
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pubmed:grant | |
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/CheW protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/methyl-accepting chemotaxis proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
235-43
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9914498-Amino Acid Sequence,
pubmed-meshheading:9914498-Bacterial Proteins,
pubmed-meshheading:9914498-Base Sequence,
pubmed-meshheading:9914498-Cyanides,
pubmed-meshheading:9914498-Desulfovibrio,
pubmed-meshheading:9914498-Evolution, Molecular,
pubmed-meshheading:9914498-Membrane Proteins,
pubmed-meshheading:9914498-Models, Molecular,
pubmed-meshheading:9914498-Molecular Sequence Data,
pubmed-meshheading:9914498-Operon,
pubmed-meshheading:9914498-Oxygen,
pubmed-meshheading:9914498-Sequence Homology, Amino Acid,
pubmed-meshheading:9914498-Signal Transduction,
pubmed-meshheading:9914498-Superoxide Dismutase
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pubmed:year |
1999
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pubmed:articleTitle |
Desulfovibrio gigas neelaredoxin. A novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe.
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pubmed:affiliation |
Instituto Gulbenkian de Ciência, Oeiras, Portugal.
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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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