The Early Interaction of the Outer Membrane Protein PhoE with the Periplasmic Chaperone Skp Occurs at the Cytoplasmic Membrane
Open Access
- 1 June 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (22) , 18804-18811
- https://doi.org/10.1074/jbc.m011194200
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activityThe EMBO Journal, 2001
- The Periplasmic Escherichia coli Peptidylprolyl cis,trans-Isomerase FkpAJournal of Biological Chemistry, 2000
- TARGETING AND ASSEMBLY OF PERIPLASMIC AND OUTER-MEMBRANE PROTEINS IN ESCHERICHIA COLIAnnual Review of Genetics, 1998
- The Sec systemCurrent Opinion in Microbiology, 1998
- Folding of a bacterial outer membrane protein during passage through the periplasmThe EMBO Journal, 1997
- Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factorMolecular Microbiology, 1997
- Protein folding in the bacterial periplasmJournal of Bacteriology, 1997
- Identification of the prolyl isomerase domain of Escherichia coli trigger factorFEBS Letters, 1996
- Biogenesis of outer membrane protein PhoE of Escherichia coli: Evidence for multiple SecB-binding sites in the mature portion of the PhoE proteinJournal of Molecular Biology, 1992
- Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.The EMBO Journal, 1989