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Cited 5 time in webofscience Cited 6 time in scopus
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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
Authors
KIM, JEONG MOKSouk, Ok-HeeHEO, JIEUNKIM, DASOMJeonghun YeomVarshavsky, AYOO, JOO YEONCheolju LeeShinyeong JuHWANG, CHEOL SANG
Date Issued
Nov-2018
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
http://oasis.postech.ac.kr/handle/2014.oak/94263
ISSN
0036-8075
Article Type
Article
Citation
SCIENCE, vol. 362, no. 6418, page. 1019 - +, 2018-11
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 HWANG, CHEOL SANG
Dept of Life Sciences
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