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2010-09-29Zeitschriftenartikel DOI: 10.1186/1471-2180-10-251
PpiD is a player in the network of periplasmic chaperones in Escherichia coli
dc.contributor.authorMatern, Yvonne
dc.contributor.authorBarion, Birgitta
dc.contributor.authorBehrens-Kneip, Susanne
dc.date.accessioned2018-05-07T14:07:37Z
dc.date.available2018-05-07T14:07:37Z
dc.date.created2010-10-19
dc.date.issued2010-09-29none
dc.identifier.otherhttp://edoc.rki.de/oa/articles/reJIRaofeg7wU/PDF/239khOYQZ7dQI.pdf
dc.identifier.urihttp://edoc.rki.de/176904/720
dc.description.abstractBackground: The inner membrane-anchored periplasmic folding factor PpiD is described as a parvulin-like peptidyl prolyl isomerase (PPIase) that assists in the maturation of the major beta-barrel outer membrane proteins (OMPs) of Escherichia coli. More recent work however, calls these findings into question. Here, we re-examined the role of PpiD in the E. coli periplasm by analyzing its functional interplay with other folding factors that influence OMP maturation as well as general protein folding in the periplasmic compartment of the cell, such as SurA, Skp, and DegP. Results: The analysis of the effects of both deletion and overexpression of ppiD on cell envelope phenotypes revealed that PpiD in contrast to prior observations plays only a minor role, if any, in the maturation of OMPs and cannot compensate for the lack of SurA in the periplasm. On the other hand, our results show that overproduction of PpiD rescues a surA skp double mutant from lethality. In the presence of increased PpiD levels surA skp cells show reduced activities of both the SigmaE-dependent and the Cpx envelope stress responses, and contain increased amounts of folded species of the major OMP OmpA. These effects require the anchoring of PpiD in the inner membrane but are independent of its parvulin-like PPIase domain. Moreover, a PpiD protein lacking the PPIase domain also complements the growth defects of an fkpA ppiD surA triple PPIase mutant and exhibits chaperone activity in vitro. In addition, PpiD appears to collaborate with DegP, as deletion of ppiD confers a temperature-dependent conditional synthetic phenotype in a degP mutant. Conclusions: This study provides first direct evidence that PpiD functions as a chaperone and contributes to the network of periplasmic chaperone activities without being specifically involved in OMP maturation. Consistent with previous work, our data support a model in which the chaperone function of PpiD is used to aid in the early periplasmic folding of many newly translocated proteins.eng
dc.language.isoeng
dc.publisherRobert Koch-Institut
dc.subjectEscherichia coli/geneticseng
dc.subjectEscherichia coli/metabolismeng
dc.subjectEscherichia coli Proteins/geneticseng
dc.subjectBacterial Outer Membrane Proteins/metabolismeng
dc.subjectBacterial Outer Membrane Proteins/geneticseng
dc.subjectCarrier Proteins/geneticseng
dc.subjectCarrier Proteins/physiologyeng
dc.subjectEscherichia coli Proteins/physiologyeng
dc.subjectMolecular Chaperones/geneticseng
dc.subjectMolecular Chaperones/physiologyeng
dc.subjectPeptidylprolyl Isomerase/geneticseng
dc.subjectPeptidylprolyl Isomerase/physiologyeng
dc.subjectPeriplasm/metabolismeng
dc.subjectProtein Foldingeng
dc.subject.ddc610 Medizin
dc.titlePpiD is a player in the network of periplasmic chaperones in Escherichia coli
dc.typeperiodicalPart
dc.identifier.urnurn:nbn:de:0257-10011032
dc.identifier.doi10.1186/1471-2180-10-251
dc.identifier.doihttp://dx.doi.org/10.25646/645
local.edoc.container-titleBMC Microbiology
local.edoc.fp-subtypeArtikel
local.edoc.type-nameZeitschriftenartikel
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-urlhttp://www.biomedcentral.com/1471-2180/10/251/abstract
local.edoc.container-publisher-nameBioMedCentral
local.edoc.container-volume10
local.edoc.container-issue251
local.edoc.container-year2010

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