Formyl-methionine as an N-degron of a eukaryotic N-end rule pathwayopen access
- Authors
- Kim, Jeong-Mok; Seok, Ok-Hee; Ju, Shinyeong; Heo, Ji-Eun; Yeom, Jeonghun; Kim, Da-Som; Yoo, Joo-Yeon; Varshavsky, Alexander; Lee, Cheolju; Hwang, Cheol-Sang
- Issue Date
- Nov-2018
- Publisher
- AMER ASSOC ADVANCEMENT SCIENCE
- Citation
- SCIENCE, v.362, no.6418, pp.1019 - +
- Indexed
- SCIE
SCOPUS
- Journal Title
- SCIENCE
- Volume
- 362
- Number
- 6418
- Start Page
- 1019
- End Page
- +
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/15978
- DOI
- 10.1126/science.aat0174
- ISSN
- 0036-8075
- 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.
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