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The chaperone‐assisted membrane release and folding pathway is sensed by two signal transduction systems
Author(s) -
Hal Jones C.,
Danese Paul N.,
Pinkner Jerome S.,
Silhavy Thomas J.,
Hultgren Scott J.
Publication year - 1997
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/16.21.6394
Subject(s) - periplasmic space , biology , chaperone (clinical) , pilus , microbiology and biotechnology , cytoplasm , protein subunit , signal transduction , protein folding , membrane protein , cell membrane , extracellular , biochemistry , biophysics , membrane , escherichia coli , gene , medicine , pathology
The assembly of interactive protein subunits into extracellular structures, such as pilus fibers in the Enterobacteriaceae, is dependent on the activity of PapD‐like periplasmic chaperones. The ability of PapD to undergo a β zippering interaction with the hydrophobic C‐terminus of pilus subunits facilitates their folding and release from the cytoplasmic membrane into the periplasm. In the absence of the chaperone, subunits remained tethered to the membrane and were driven off‐pathway via non‐productive interactions. These off‐pathway reactions were detrimental to cell growth; wild‐type growth was restored by co‐expression of PapD. Subunit misfolding in the absence of PapD was sensed by two parallel pathways: the Cpx two‐component signaling system and the σE modulatory pathway.