PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

ABSTRACT:

Background

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

SUBMITTER: Matern Y 

PROVIDER: S-EPMC2956729 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature