Work

Effect of chaperone‐adhesin complex on plug release by the PapC usher

Year: 2016

Type: article

Abstract: 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.

Source: FEBS Letters

DOI: 10.1002/1873-3468.12257

Authors: Thieng Pham, Glenn T. Werneburg, Nadine S. Henderson, David G. Thanassi, Anne H. Delcour

Institutions: University of Houston, Stony Brook University

Language: English

Topic: Escherichia coli research studies

Subfield: Endocrinology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases

Awards: G1263639037, Catalytic mechanism of the usher in pilus biogenesis by uropathogenic E. coli, G9000061531