Dynamic periplasmic chaperone reservoir facilitates biogenesis of outer membrane proteins
Author(s) -
Shawn M. Costello,
Ashlee M. Plummer,
Patrick J. Fleming,
Karen G. Fleming
Publication year - 2016
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1601002113
Subject(s) - proteostasis , periplasmic space , biogenesis , bacterial outer membrane , microbiology and biotechnology , chaperone (clinical) , protein folding , biology , membrane protein , transport protein , inner membrane , biophysics , biochemistry , membrane , mitochondrion , medicine , escherichia coli , pathology , gene
Significance The study of bacterial outer membrane proteins (OMPs) is critical to understanding cellular communication, metabolic transport across membranes, and pathogenesis. We used a holistic computational approach to examine how the OMP biogenesis machinery maintains cellular proteostasis under biologically relevant conditions. This treatment overcomes common limitations of both in vitro and in vivo experiments because we can simultaneously investigate unfolded OMP (uOMP) transport and folding trajectories at a microscopic level and phenotypes at a macroscopic level. This analysis provides global insight into the dynamic process of periplasmic uOMP transport and highlights the unique contributions of individual chaperones in the maintenance of outer membrane and periplasmic proteostasis.
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