期刊
SCIENCE
卷 359, 期 6376, 页码 689-692出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar3607
关键词
-
资金
- Howard Hughes Medical Institute
- NIH [R01AG041826, P50GM102706, R01GM062942, R01GM097432, R01GM106019]
- NSF Graduate Research Fellowship [1144247]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM097432, R01GM106019, R37GM097432, P50GM102706, T32GM007377, R01GM062942] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON AGING [R01AG041826] Funding Source: NIH RePORTER
The signal recognition particle (SRP) enables cotranslational delivery of proteins for translocation into the endoplasmic reticulum (ER), but its full in vivo role remains incompletely explored. We combined rapid auxin-induced SRP degradation with proximity-specific ribosome profiling to define SRP's in vivo function in yeast. Despite the classic view that SRP recognizes amino-terminal signal sequences, we show that SRP was generally essential for targeting transmembrane domains regardless of their position relative to the amino terminus. By contrast, many proteins containing cleavable amino-terminal signal peptides were efficiently cotranslationally targeted in SRP's absence. We also reveal an unanticipated consequence of SRP loss: Transcripts normally targeted to the ER were mistargeted to mitochondria, leading to mitochondrial defects. These results elucidate SRP's essential roles in maintaining the efficiency and specificity of protein targeting.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据