Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway
- Title
- Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway
- Author
- 김정목
- Keywords
- E3 UBIQUITIN LIGASE; HISTONE H3 VARIANT; TERMINAL ACETYLATION; STRUCTURAL BASIS; SACCHAROMYCES-CEREVISIAE; FLUORESCENT PROTEINS; CELLULAR-PROTEINS; TRANSFER-RNA; DEGRADATION; RECOGNITION
- Issue Date
- 2018-11
- Publisher
- AMER ASSOC ADVANCEMENT SCIENCE
- Citation
- SCIENCE, v. 362, no. 6418, page. 1019-+, Article no. eaat0174
- 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://science.sciencemag.org/content/362/6418/eaat0174https://repository.hanyang.ac.kr/handle/20.500.11754/120629
- ISSN
- 0036-8075; 1095-9203
- DOI
- 10.1126/science.aat0174
- Appears in Collections:
- COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > LIFE SCIENCE(생명과학과) > Articles
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