Linked Life Data

21165649

Source:http://linkedlifedata.com/resource/pubmed/id/21165649

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-1-26
pubmed:databankReference
pubmed:abstractText
The motor proteins around the flagellar basal body consist of two cytoplasmic membrane proteins, MotA and MotB, and function as a complex that acts as the stator to generate the torque that drives rotation. Genome analysis of several Pseudomonas syringae pathovars revealed that there are two sets of genes encoding motor proteins: motAB and motCD. Deduced amino acid sequences for MotA/B and MotC/D showed homologies to the H(+)-driven stator from Escherichia coli and Na(+)-driven stator from Vibrio alginolyticus, respectively. However, the swimming motility of P. syringae pv. tabaci (Pta) 6605 was inhibited by the protonophore carbonyl cyanide m-chlorophenylhydrazone but not by the sodium stator-specific inhibitor phenamil. To identify a gene encoding the stator protein required for motility, ?motAB, ?motCD, and ?motABCD mutants were generated. The ?motCD mutant had remarkably reduced and the ?motABCD mutant completely abolished swimming motilities, whereas the ?motAB mutant retained some degree of these abilities. The ?motCD and ?motABCD mutants did not produce N-acyl-homoserine lactones (AHLs), quorum-sensing molecules in this pathogen, and remarkably reduced the ability to cause disease in host tobacco leaves, as we previously observed in the ?fliC mutant strain. These results strongly indicate that both stator pairs in Pta 6605 are proton-dependent and that MotCD is important for not only flagellar motility but also for production of AHLs and the ability to cause disease in host plants.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1617-4623
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
285
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
163-74
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Two flagellar stators and their roles in motility and virulence in Pseudomonas syringae pv. tabaci 6605.
pubmed:affiliation
Graduate School of Natural Science and Technology, Okayama University, 1-1-1 Tsushima-naka, Kita-ku, Okayama 700-8530, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't