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Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway.

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.

SUBMITTER: Kim JM 

PROVIDER: S-EPMC6551516 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway.

Kim Jeong-Mok JM   Seok Ok-Hee OH   Ju Shinyeong S   Heo Ji-Eun JE   Yeom Jeonghun J   Kim Da-Som DS   Yoo Joo-Yeon JY   Varshavsky Alexander A   Lee Cheolju C   Hwang Cheol-Sang CS  

Science (New York, N.Y.) 20181108 6418

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-reg  ...[more]

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