Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 111, Issue 13, Pages 4844-4849Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1315901111
Keywords
-
Categories
Funding
- Royal Society Leverhulme Research Fellowship
- Biotechnology and Biological Sciences Research Council [BB/F007248/1, BB/I008675/1]
- Baden-Wurttemberg Stiftung
- Agence Nationale de la Recherche (HOLOTRANS project) [JC09_471873]
- European Research Council Starting Grant [281331]
- European Commission Framework Programme 7 project ComplexINC [279039]
- Biotechnology and Biological Sciences Research Council [974636, BB/F007248/1, BB/I008675/1] Funding Source: researchfish
- European Research Council (ERC) [281331] Funding Source: European Research Council (ERC)
- BBSRC [BB/I008675/1, BB/F007248/1] Funding Source: UKRI
Ask authors/readers for more resources
The SecY/61 complex forms the protein-channel component of the ubiquitous protein secretion and membrane protein insertion apparatus. The bacterial version SecYEG interacts with the highly conserved YidC and SecDF-YajC subcomplex, which facilitates translocation into and across the membrane. Together, they form the holo-translocon (HTL), which we have successfully over-expressed and purified. In contrast to the homo-dimeric SecYEG, the HTL is a hetero-dimer composed of single copies of SecYEG and SecDF-YajC-YidC. The activities of the HTL differ from the archetypal SecYEG complex. It is more effective in cotranslational insertion of membrane proteins and the posttranslational secretion of a beta-barreled outer-membrane protein driven by SecA and ATP becomes much more dependent on the proton-motive force. The activity of the translocating copy of SecYEG may therefore be modulated by association with different accessory subcomplexes: SecYEG (forming SecYEG dimers) or SecDF-YajC-YidC (forming the HTL). This versatility may provide a means to refine the secretion and insertion capabilities according to the substrate. A similar modularity may also be exploited for the translocation or insertion of a wide range of substrates across and into the endoplasmic reticular and mitochondrial membranes of eukaryotes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available