YaeT-independent multimerization and outer membrane association of secretin PulD.
Mol Microbiol
; 64(5): 1350-7, 2007 Jun.
Article
in En
| MEDLINE
| ID: mdl-17542925
ABSTRACT
Previous studies demonstrated that targeting of the dodecameric secretin PulD to the Escherichia coli outer membrane is strictly dependent on the chaperone-like pilotin PulS. Here, we report that PulD multimerization and membrane association in strains producing PulS were unaffected when the levels of the essential outer membrane assembly factor YaeT(Omp85) were reduced by controlled expression of a paraBAD-yaeT transcriptional fusion. This behaviour contrasted markedly to that of the trimeric porin LamB, which remained monomeric under these conditions. Furthermore, resistance to extraction by the detergent Sarkosyl and by urea, and susceptibility to trypsin digestion all suggested that PulD localized to the outer membrane in YaeT-depleted cells. We conclude that, unlike classical beta-barrel outer membrane proteins such as LamB, multimerization of PulD is largely YaeT-independent.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Outer Membrane Proteins
/
Cell Membrane
/
Escherichia coli Proteins
Type of study:
Risk_factors_studies
Language:
En
Journal:
Mol Microbiol
Journal subject:
BIOLOGIA MOLECULAR
/
MICROBIOLOGIA
Year:
2007
Document type:
Article
Affiliation country:
Francia