Secretion of beta-lactamase into the periplasm of Escherichia coli: evidence for a distinct release step associated with a conformational change.
- 1 June 1986
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 83 (12) , 4180-4184
- https://doi.org/10.1073/pnas.83.12.4180
Abstract
The secretion of .beta.-lactamase (EC 3.5.2.6) into the periplasm of Escherichia coli has been followed by pulse-chase labeling at 15.degree. C. Though the periplasmic fraction contains only the mature form of the enzyme, the spheroplast fraction contains the completed precursor and a hitherto undocumented processed form. When whole spheroplasts are treated with trypsin, the processed form in this fraction is completely digested. This is in contrast to the native mature enzyme localized in the periplasm, which is trypsin resistant. The .beta.-lactamase is evidently processed after translocation to a trypsin-sensitive form that is transiently bound to the periplasmic face of the inner membrane. The release of this processed form into the periplasm occurs concomitantly with a conformational change that results in the soluble, catalytically active, trypsin-resistant structure.This publication has 23 references indexed in Scilit:
- Export of protein in bacteria.1984
- Protein translocation across the endoplasmic reticulumCell, 1984
- D-ribose metabolism in Escherichia coli K-12: genetics, regulation, and transportJournal of Bacteriology, 1984
- The role of the beta-lactamase signal sequence in the secretion of proteins by Escherichia coli.Journal of Biological Chemistry, 1984
- Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongationCell, 1983
- Evidence for posttranslational translocation of β-lactamase across the bacterial inner membraneCell, 1982
- Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.The Journal of cell biology, 1981
- Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein.The Journal of cell biology, 1981
- Different exported proteins in E. coli show differences in the temporal mode of processing in vivoCell, 1981
- Role of the mature protein sequence of maltose-binding protein in its secretion across the E. coli cytoplasmic membraneCell, 1981