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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1997-3-18
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pubmed:databankReference |
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pubmed:abstractText |
The Rhodobacter sphaeroides mutants Drn12 and Drn21 derepressed for nitrogenase synthesis in the presence of ammonia and impaired in utilization of certain nitrogen sources have been analyzed. Both mutants show a low level of expression of the glnBA operon. The DNA fragment restoring the wild-type phenotype to these mutants contains the 3'-portion of ntrB gene and the entire ntrC gene. Sequence analysis showed that Drn12 bears a missense mutation in the ntrC gene. The mutation results in the replacement of a glycine residue by aspartate within the N-terminal domain of the NtrC protein. Pleiotropic phenotypes of Drn12 and Drn21 appear to be associated with an alteration in the regulation of glnBA expression.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate-Ammonia Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamine,
http://linkedlifedata.com/resource/pubmed/chemical/Methylamines,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/PII Nitrogen Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Quaternary Ammonium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/glutamine synthetase I,
http://linkedlifedata.com/resource/pubmed/chemical/methylamine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0378-1097
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
147
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
57-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9037764-Bacterial Proteins,
pubmed-meshheading:9037764-Cloning, Molecular,
pubmed-meshheading:9037764-DNA-Binding Proteins,
pubmed-meshheading:9037764-Gene Expression Regulation, Bacterial,
pubmed-meshheading:9037764-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:9037764-Genes, Bacterial,
pubmed-meshheading:9037764-Glutamate-Ammonia Ligase,
pubmed-meshheading:9037764-Glutamine,
pubmed-meshheading:9037764-Methylamines,
pubmed-meshheading:9037764-Mutation,
pubmed-meshheading:9037764-Nitrogen,
pubmed-meshheading:9037764-Nitrogenase,
pubmed-meshheading:9037764-Open Reading Frames,
pubmed-meshheading:9037764-PII Nitrogen Regulatory Proteins,
pubmed-meshheading:9037764-Plasmids,
pubmed-meshheading:9037764-Quaternary Ammonium Compounds,
pubmed-meshheading:9037764-Rhodobacter sphaeroides,
pubmed-meshheading:9037764-Sequence Analysis, DNA,
pubmed-meshheading:9037764-Trans-Activators,
pubmed-meshheading:9037764-Transcription Factors
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pubmed:year |
1997
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pubmed:articleTitle |
Mutation in ntrC gene leading to the derepression of nitrogenase synthesis in Rhodobacter sphaeroides.
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pubmed:affiliation |
Department of Genetics, Moscow State University, Russia. vzin@string.stringer.ru
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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