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The pioneer round of translation ensures proper targeting of ER and mitochondrial proteins

Authors
Park, JooriChang, JeeyoonHwang, Hyun JungJeong, KwonLee, Hyuk-JoonHa, HongseokPark, YeonkyoungLim, ChunghunWoo, Jae-SungKim, Yoon Ki
Issue Date
2-12월-2021
Publisher
OXFORD UNIV PRESS
Citation
NUCLEIC ACIDS RESEARCH, v.49, no.21, pp.12517 - 12534
Indexed
SCIE
SCOPUS
Journal Title
NUCLEIC ACIDS RESEARCH
Volume
49
Number
21
Start Page
12517
End Page
12534
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/135478
DOI
10.1093/nar/gkab1098
ISSN
0305-1048
Abstract
The pioneer (or first) round of translation of newly synthesized mRNAs is largely mediated by a nuclear cap-binding complex (CBC). In a transcriptome-wide analysis of polysome-associated and CBC-bound transcripts, we identify RN7SL1, a noncoding RNA component of a signal recognition particle (SRP), as an interaction partner of the CBC. The direct CBC-SRP interaction safeguards against abnormal expression of polypeptides from a ribosome-nascent chain complex (RNC)-SRP complex until the latter is properly delivered to the endoplasmic reticulum. Failure of this surveillance causes abnormal expression of misfolded proteins at inappropriate intracellular locations, leading to a cytosolic stress response. This surveillance pathway also blocks protein synthesis through RNC-SRP misassembled on an mRNA encoding a mitochondrial protein. Thus, our results reveal a surveillance pathway in which pioneer translation ensures proper targeting of endoplasmic reticulum and mitochondrial proteins.
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Graduate School > Department of Life Sciences > 1. Journal Articles
College of Life Sciences and Biotechnology > Division of Life Sciences > 1. Journal Articles

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