한빛사 논문
Joori Park1,2,†, Jeeyoon Chang1,2,†, Hyun Jung Hwang1,2, Kwon Jeong1,2, Hyuk-Joon Lee2, Hongseok Ha1,2, Yeonkyoung Park1,2, Chunghun Lim3, Jae-Sung Woo2 and Yoon Ki Kim1,2,*
1Creative Research Initiatives Center for Molecular Biology of Translation, Korea University, Seoul 02841, Republic of Korea, 2Division of Life Sciences, Korea University, Seoul 02841, Republic of Korea and 3School of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan 44919, Republic of Korea
*To whom correspondence should be addressed.
†The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint first authors.
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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