共 40 条
AN ATP-BINDING MEMBRANE-PROTEIN IS REQUIRED FOR PROTEIN TRANSLOCATION ACROSS THE ENDOPLASMIC-RETICULUM MEMBRANE
被引:17
作者:
ZIMMERMAN, DL
WALTER, P
机构:
[1] Dept. of Biochemistry and Biophysics, University of California, Medical School, San Francisco
来源:
CELL REGULATION
|
1991年
/
2卷
/
10期
关键词:
D O I:
10.1091/mbc.2.10.851
中图分类号:
Q2 [细胞生物学];
学科分类号:
071009 ;
090102 ;
摘要:
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-P-32]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.
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页码:851 / 859
页数:9
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