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Effect of chaperone‐adhesin complex on plug release by the PapC usher
Author(s) -
Pham Thieng,
Werneburg Glenn T.,
Henderson Nadine S.,
Thanassi David G.,
Delcour Anne H.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12257
Subject(s) - periplasmic space , chaperone (clinical) , bacterial outer membrane , pilus , bacterial adhesin , escherichia coli , biology , protein subunit , microbiology and biotechnology , fimbria , biogenesis , biophysics , biochemistry , gene , medicine , pathology
The P pilus of uropathogenic Escherichia coli is a multisubunit fiber assembled at the outer membrane in a defined sequence by a chaperone/usher secretion system, comprising a periplasmic chaperone and a beta‐barrel outer membrane protein, the PapC usher. To gain insight into the pilus biogenesis mechanism, we used patch clamp electrophysiology to investigate the effect of the initiating adhesin subunit, as it is delivered to PapC in a complex with the chaperone. We show that the chaperone‐adhesin complex facilitates opening of the PapC pore and appears to engage within the PapC lumen, in agreement with prior biochemical and structural data.