YidC mediates membrane protein insertion in bacteria Journal Article
| Authors: | Samuelson, J. C.; Chen, M.; Jiang, F.; Moller, I.; Wiedmann, M.; Kuhn, A.; Phillips, G. J.; Dalbey, R. E. |
| Article Title: | YidC mediates membrane protein insertion in bacteria |
| Abstract: | The basic machinery for the translocation of proteins into or across membranes is remarkably conserved from Escherichia coli to humans. In eukaryotes, proteins are inserted into the endoplasmic reticulum using the signal recognition particle (SRP) and the SRP receptor, as well as the integral membrane Sec61 trimeric complex (composed of alpha, beta and gamma subunits). In bacteria, most proteins are inserted by a related pathway that includes the SRP homologue Ffh, the SRP receptor FtsY, and the SecYEG trimeric complex, where Y and E are related to the Sec61 alpha and gamma subunits, respectively. Proteins in bacteria that exhibit no dependence on the Sec translocase were previously thought to insert into the membrane directly without the aid of a protein machinery.-Here we show that membrane insertion of two Sec-independent proteins requires YidC. YidC is essential for E. coli viability and homologues are present in mitochondria and chloroplasts. Depletion of YidC also interferes with insertion of Sec-dependent membrane proteins, but it has only a minor effect on the export of secretory proteins. These results provide evidence for an additional component of the translocation machinery that is specialized for the integration of membrane proteins. |
| Keywords: | carrier protein; nonhuman; cell viability; atp-binding cassette transporters; membrane proteins; nuclear proteins; endoplasmic reticulum; bacterial proteins; protein processing, post-translational; serine endopeptidases; escherichia coli; carrier proteins; membrane protein; cell membrane; protein transport; gene insertion; mitochondrion; biological transport; escherichia coli proteins; bacterial outer membrane proteins; capsid; protein precursors; mitochondrial proteins; cross-linking reagents; membrane transport proteins; bacterial membrane; secretory protein; capsid proteins; electron transport complex iv; monosaccharide transport proteins; signal recognition particle; priority journal; article; chloroplast |
| Journal Title: | Nature |
| Volume: | 406 |
| Issue: | 6796 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2000-08-10 |
| Start Page: | 637 |
| End Page: | 641 |
| Language: | English |
| DOI: | 10.1038/35020586 |
| PUBMED: | 10949305 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 18 November 2015 -- Source: Scopus |
Altmetric
Citation Impact
BMJ Impact Analytics
Related MSK Work