Export of Periplasmic Galactose-binding Protein in Escherichia Coli Depends on the Chaperone SecB
Overview
Authors
Affiliations
The efficient export of galactose-binding protein to the periplasm of Escherichia coli is shown to be dependent on the presence of the cytosolic chaperone SecB.
Coassembly of SecYEG and SecA Fully Restores the Properties of the Native Translocon.
Bariya P, Randall L J Bacteriol. 2018; 201(1).
PMID: 30275279 PMC: 6287467. DOI: 10.1128/JB.00493-18.
The Sec System: Protein Export in .
Crane J, Randall L EcoSal Plus. 2017; 7(2).
PMID: 29165233 PMC: 5807066. DOI: 10.1128/ecosalplus.ESP-0002-2017.
Determination of the intracellular concentration of the export chaperone SecB in Escherichia coli.
Findik B, Randall L PLoS One. 2017; 12(8):e0183231.
PMID: 28850586 PMC: 5574556. DOI: 10.1371/journal.pone.0183231.
Multitasking SecB chaperones in bacteria.
Sala A, Bordes P, Genevaux P Front Microbiol. 2014; 5:666.
PMID: 25538690 PMC: 4257090. DOI: 10.3389/fmicb.2014.00666.
Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.
Mao C, Cheadle C, Hardy S, Lilly A, Suo Y, Sanganna Gari R Proc Natl Acad Sci U S A. 2013; 110(29):11815-20.
PMID: 23818593 PMC: 3718118. DOI: 10.1073/pnas.1303289110.