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rdf:type |
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lifeskim:mentions |
umls-concept:C0008142,
umls-concept:C0017337,
umls-concept:C0679058,
umls-concept:C0752020,
umls-concept:C0851827,
umls-concept:C1160177,
umls-concept:C1305923,
umls-concept:C1334043,
umls-concept:C1547699,
umls-concept:C1701901,
umls-concept:C2700640
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pubmed:issue |
23
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pubmed:dateCreated |
1997-1-28
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pubmed:databankReference |
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pubmed:abstractText |
Stigmatella aurantiaca is a prokaryotic organism that undergoes a multicellular cycle of development resulting in the formation of a fruiting body. For analyzing this process, mutants defective in fruiting body formation have been induced by transposon mutagenesis using a Tn5-derived transposon. About 800 bp upstream of the transposon insertion of mutant AP182 which inactivates a gene (fbfB) involved in fruiting, a further gene (fbfA) needed for fruiting body formation was detected. Inactivation of fbfA leads to mutants which form only non-structured clumps instead of the wild-type fruiting body. The mutant phenotype of fbfA mutants can be partially suppressed by mixing the mutant cells with cells of some independent mutants defective in fruiting body formation. The fbfA gene is transcribed after 8 h of development as determined by measuring the induction of beta-galactosidase activity of a fbfA-delta(trp)-lacZ fusion gene and by Northern (RNA) analysis using an insertion encoding a stable mRNA. The predicted polypeptide FbfA shows a homology of about 30% to NodC of rhizobia, an N-acetylglucosamine-transferase which is involved in the synthesis of the sugar backbone of lipo-oligosaccharides. These induce the formation of the root nodules in the Papilionaceae. Besides the predicted molecular mass of 45.5 kDa, the hydropathy profile reveals a structural relationship to the NodC polypeptide.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-109333,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-1427102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-1475843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-15929218,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-2116988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-2172217,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-2440339,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-6336331,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-6514582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-7592395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-7692215,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-7775457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-7815941,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-7934859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-8146173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-8366070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-8431309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-8432741,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-8509650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-8852896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8955286-96528
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
178
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6706-13
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:8955286-Amino Acid Sequence,
pubmed-meshheading:8955286-Bacterial Proteins,
pubmed-meshheading:8955286-Base Sequence,
pubmed-meshheading:8955286-Chitin Synthase,
pubmed-meshheading:8955286-DNA Transposable Elements,
pubmed-meshheading:8955286-Gene Expression,
pubmed-meshheading:8955286-Genes, Bacterial,
pubmed-meshheading:8955286-Molecular Sequence Data,
pubmed-meshheading:8955286-Molecular Weight,
pubmed-meshheading:8955286-Mutagenesis, Insertional,
pubmed-meshheading:8955286-Myxococcales,
pubmed-meshheading:8955286-N-Acetylglucosaminyltransferases,
pubmed-meshheading:8955286-Sequence Alignment,
pubmed-meshheading:8955286-Transcription, Genetic
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pubmed:year |
1996
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pubmed:articleTitle |
Stigmatella aurantiaca fruiting body formation is dependent on the fbfA gene encoding a polypeptide homologous to chitin synthases.
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pubmed:affiliation |
Zentrum für Molekulare Biologie der Universität Heidelberg, Germany.
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pubmed:publicationType |
Journal Article
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