期刊
CELL
卷 100, 期 3, 页码 333-343出版社
CELL PRESS
DOI: 10.1016/S0092-8674(00)80669-8
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资金
- NIGMS NIH HHS [GM 35687] Funding Source: Medline
Targeting of ribosome-nascent chain complexes to the translocon in the endoplasmic reticulum is mediated by the concerted action of the signal recognition particle (SRP) and the SRP receptor (SR). Ribosome-stripped microsomes were digested with proteases to sever cytoplasmic domains of SR alpha, SR beta, TRAM, and the Sec61 complex. We characterized protein translocation intermediates that accumulate when Sec61 alpha or SRP is inactivated by proteolysis. In the absence of a functional Sec61 complex, dissociation of SRP54 from the signal sequence is blocked. Experiments using SR proteoliposomes confirmed the assembly of a membrane-bound posttargeting intermediate. These results strongly suggest that the Sec61 complex regulates the GTP hydrolysis cycle of the SRP-SR complex at the stage of signal sequence dissociation from SRP54.
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