Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway
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SCOPUS
- Title
- Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway
- Authors
- KIM, JEONG MOK; Souk, Ok-Hee; HEO, JIEUN; KIM, DASOM; Jeonghun Yeom; Varshavsky, A; YOO, JOO YEON; Cheolju Lee; Shinyeong Ju; HWANG, CHEOL SANG
- Date Issued
- 2018-11
- Publisher
- AMER ASSOC ADVANCEMENT SCIENCE
- Abstract
- In bacteria, nascent proteins bear the pretranslationally generated N-terminal (Nt) formyl-methionine (fMet) residue. Nt-fMet of bacterial proteins is a degradation signal, termed fMet/N-degron. By contrast, proteins synthesized by cytosolic ribosomes of eukaryotes were presumed to bear unformylated Nt-Met. Here we found that the yeast formyltransferase Fmt1, although imported into mitochondria, could also produce Nt-formylated proteins in the cytosol. Nt-formylated proteins were strongly up-regulated in stationary phase or upon starvation for specific amino acids. This up-regulation strictly required the Gcn2 kinase, which phosphorylates Fmt1 and mediates its retention in the cytosol. We also found that the Nt-fMet residues of Nt-formylated proteins act as fMet/N-degrons and identified the Psh1 ubiquitin ligase as the recognition component of the eukaryotic fMet/N-end rule pathway, which destroys Nt-formylated proteins.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/94263
- DOI
- 10.1126/science.aat0174
- ISSN
- 0036-8075
- Article Type
- Article
- Citation
- SCIENCE, vol. 362, no. 6418, page. 1019 - +, 2018-11
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- There are no files associated with this item.
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