Abstract
The role of nucleotides in providing energy for polypeptide transfer across the endoplasmic reticulum (ER) membrane is still unknown. To address this question, we treated ER-derived mammalian microsomal vesicles with a photoactivatable analogue of ATP, 8-N3ATP. This treatment resulted in a progressive inhibition of translocation activity. Approximately 20 microsomal membrane proteins were labeled by [alpha 32P]8-N3ATP. Two of these were identified as proteins with putative roles in translocation, alpha signal sequence receptor (SSR), the 35-kDa subunit of the signal sequence receptor complex, and ER-p180, a putative ribosome receptor. We found that there was a positive correlation between inactivation of translocation activity and photolabeling of alpha SSR. In contrast, our data demonstrate that the ATP-binding domain of ER-p180 is dispensable for translocation activity and does not contribute to the observed 8-N3ATP sensitivity of the microsomal vesicles.
Dates
Type | When |
---|---|
Created | 12 years ago (Aug. 16, 2013, 6:42 p.m.) |
Deposited | 6 years, 1 month ago (July 14, 2019, 11:09 a.m.) |
Indexed | 1 year, 7 months ago (Jan. 10, 2024, 5 p.m.) |
Issued | 33 years, 10 months ago (Oct. 1, 1991) |
Published | 33 years, 10 months ago (Oct. 1, 1991) |
Published Print | 33 years, 10 months ago (Oct. 1, 1991) |
@article{Zimmerman_1991, title={An ATP-binding membrane protein is required for protein translocation across the endoplasmic reticulum membrane.}, volume={2}, ISSN={1044-2030}, url={http://dx.doi.org/10.1091/mbc.2.10.851}, DOI={10.1091/mbc.2.10.851}, number={10}, journal={Cell Regulation}, publisher={American Society for Cell Biology (ASCB)}, author={Zimmerman, D L and Walter, P}, year={1991}, month=oct, pages={851–859} }