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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-4-29
pubmed:abstractText
Protein secretion in gram-negative bacteria is often dependent on the general secretory pathway (GSP). In Pseudomonas aeruginosa, this system requires at least 12 Xcp (Gsp) proteins, which are proposed to constitute a multiprotein complex localized in the bacterial envelope. Hitherto, little was known about the mutual interactions between Xcp proteins. In this study, mutants affected in the xcpZ gene encoding a bitopic inner-membrane protein were analysed to investigate the role of this protein in the architecture of the secretory machinery. The absence of XcpZ resulted in a decreased amount of XcpY. Reciprocally, XcpZ was not detectable in a xcpY mutant, demonstrating a mutual stabilization of these two proteins. These results strongly suggest that XcpZ and XcpY interact within the functional secretory apparatus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
144 ( Pt 12)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3379-86
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa.
pubmed:affiliation
Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UPR9027, IBSM/CNRS, Marseille, France. michel@ibsm.cnrs-mrs.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't