Identification of putative substrates for the periplasmic chaperone YfgM in Escherichia coli using quantitative proteomics.

ABSTRACT: How proteins are trafficked, folded, and assembled into functional units in the cell envelope of Gram-negative bacteria is of significant interest. A number of chaperones have been identified, however, the molecular roles of these chaperones are often enigmatic because it has been challenging to assign substrates. Recently we discovered a novel periplasmic chaperone, called YfgM, which associates with PpiD and the SecYEG translocon and operates in a network that contains Skp and SurA. The aim of the study presented here was to identify putative substrates of YfgM. We reasoned that substrates would be incorrectly folded or trafficked when YfgM was absent from the cell, and thus more prone to proteolysis (the loss-of-function rationale). We therefore used a comparative proteomic approach to

SUBMITTER: Gotzke H 

PROVIDER: S-EPMC4288256 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature