Protein export in Escherichia coli requires a soluble activity.
- 1 December 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (24), 7737-7741
- https://doi.org/10.1073/pnas.81.24.7737
Abstract
A reconstituted cell-free system was used to demonstrate the existence of a soluble activity that is required for the export of proteins in E. coli. This export factor sediments at .apprx. 12 S. It has been partially purified by passage through an .omega.-NH2-butylagarose column and by salt elution off a DEAE matrix. The export factor does not contain 6S RNA.This publication has 26 references indexed in Scilit:
- The product of gene secC is involved in the synthesis of exported proteins in E. coliCell, 1984
- Subcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probe.The Journal of cell biology, 1983
- Disassembly and reconstitution of signal recognition particleCell, 1983
- Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulumNature, 1982
- Mechanism of Incorporation of Cell Envelope Proteins in Escherichia ColiAnnual Review of Microbiology, 1982
- Regulation of a membrane component required for protein secretion in escherichia coliCell, 1982
- Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.The Journal of cell biology, 1981
- 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
- Purification and characterization of protein synthesis initiation factors IF1, IF2, and IF3 from Escherichia coliArchives of Biochemistry and Biophysics, 1977