Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-11-15
pubmed:abstractText
In Bacillus subtilis, the ComQXPA quorum-sensing system controls cell density-dependent phenotypes such as the production of degradative enzymes and antibiotics and the development of genetic competence. Bacillus subtilis (natto) NAF12, a mutant defective in poly-gamma-glutamate (gamma-PGA) production, was derived from B. subtilis (natto) NAF4 by Tn917-LTV1 insertional mutagenesis. Determination of the mutant DNA sequences flanking the Tn917-LTV1 insert revealed that the insertion had inactivated comP in this mutant, indicating that gamma-PGA synthesis in B. subtilis (natto) is under the control of the ComP-ComA signal transduction system. A comparison of the amino acid sequences revealed striking variation in the primary structures of ComQ (44% identity), ComX (26%) and the sensor domain of ComP (36%) between B. subtilis (natto) NAF4 and B. subtilis 168. In contrast, the amino acid and nucleotide sequences of the kinase domains of ComP and of the ComA response regulator share 95% and 100% identity respectively. The comP genes of NAF4 and 168 restored the impaired competence of B. subtilis BD1658 (comP:cat) and gamma-PGA production of B. subtilis (natto) NAF12 (comP:Tn917-LTV1) to only 15% of the level achieved by the respective parent comP genes. However, when introduced together with the cognate comQ and comX genes, the comP genes restored the relevant defect of the heterologous comP mutants nearly to wild-type levels. Analogous to the comCDE system of Streptococcus strains and the agrBCDE system of Staphylococcus aureus, the concerted variation in the comQXP genes appears to establish specific intercellular communication between B. subtilis strains sharing the same pheromone system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ComA protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/ComX protein, Bacillus subtilis, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Synthases, http://linkedlifedata.com/resource/pubmed/chemical/Pheromones, http://linkedlifedata.com/resource/pubmed/chemical/Polyglutamic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Transferases, http://linkedlifedata.com/resource/pubmed/chemical/comP protein, Bacillus subtilis, http://linkedlifedata.com/resource/pubmed/chemical/comQ protein, Bacillus subtilis, http://linkedlifedata.com/resource/pubmed/chemical/surfactin synthetase
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1159-71
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10972833-Amino Acid Sequence, pubmed-meshheading:10972833-Artificial Gene Fusion, pubmed-meshheading:10972833-Bacillus subtilis, pubmed-meshheading:10972833-Bacterial Proteins, pubmed-meshheading:10972833-Base Sequence, pubmed-meshheading:10972833-DNA, Bacterial, pubmed-meshheading:10972833-DNA-Binding Proteins, pubmed-meshheading:10972833-Enzyme Induction, pubmed-meshheading:10972833-Genes, Bacterial, pubmed-meshheading:10972833-Humans, pubmed-meshheading:10972833-Lac Operon, pubmed-meshheading:10972833-Membrane Proteins, pubmed-meshheading:10972833-Molecular Sequence Data, pubmed-meshheading:10972833-Peptide Synthases, pubmed-meshheading:10972833-Pheromones, pubmed-meshheading:10972833-Polyglutamic Acid, pubmed-meshheading:10972833-Sequence Homology, Amino Acid, pubmed-meshheading:10972833-Transferases
pubmed:year
2000
pubmed:articleTitle
Divergent structure of the ComQXPA quorum-sensing components: molecular basis of strain-specific communication mechanism in Bacillus subtilis.
pubmed:affiliation
Division of Applied Microbiology, National Food Research Institute, Ministry of Agriculture, Forestry and Fisheries, Kannondai 2-1-2, Tsukuba 305-8642, Japan.
pubmed:publicationType
Journal Article