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N-terminal formylmethionine as a novel initiator and N-degron of eukaryotic proteins

Title
N-terminal formylmethionine as a novel initiator and N-degron of eukaryotic proteins
Author
김정목
Keywords
Formyltransferase; Gcn2; Methionine; Proteolysis; Psh1; Ubiquitin
Issue Date
2019-03
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Citation
BMB REPORTS, v. 52, NO 3, Page. 163-164
Abstract
The ribosomal synthesis of proteins in the eukaryotic cytosol has always been thought to start from the unfomiylated N-terminal (Nt) methionine (Met). In contrast, in virtually all nascent proteins in bacteria and eukaryotic organelles, such as mitochondria and chloroplasts, Nt-formyl-methionine (fMet) is the first building block of ribosomal synthesis. Through extensive approaches, including mass spectrometric analyses of the N-terrnini of proteins and molecular genetic techniques with an affinity-purified antibody for Nt-formylation, we investigated whether Nt-formylated proteins could also be produced and have their own metabolic fate in the cytosol of a eukaryote, such as yeast Saccharomyces cerevisiae. We discovered that Nt-foimylated proteins could be generated in the cytosol by yeast mitochondrial formyltransferase (Fmt1). These Nt-foimylated proteins were massively upregulated in the stationary phase or upon starvation for specific amino acids and were crucial for the adaptation to specific stresses. The stress-activated kinase Gcn2 was strictly required for the upregulation of Nt-formylated proteins by regulating the activity of Fmt1 and its retention in the cytosol. We also found that the Nt-fMet residues of Nt-foimylated proteins could be distinct N-terminal degradation signals, termed fMet/N-degrons, and that Psh1 E3 ubiquitin ligase mediated the selective destrution of Nt-foimylated proteins as the recognition component of a novel eukaryotic fMet/N-end rule pathway, termed fMet/N-recognin.
URI
http://www.bmbreports.org/journal/view.html?doi=10.5483/BMBRep.2019.52.3.069http://repository.hanyang.ac.kr/handle/20.500.11754/108551
ISSN
1976-6696; 1976-670X
DOI
10.5483/BMBRep.2019.52.3.069
Appears in Collections:
COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > LIFE SCIENCE(생명과학과) > Articles
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