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- Title
Methylglyoxal activates Gcn2 to phosphorylate eIF2α independently of the TOR pathway in Saccharomyces cerevisiae.
- Authors
Nomura, Wataru; Maeta, Kazuhiro; Kita, Keiko; Izawa, Shingo; Inoue, Yoshiharu
- Abstract
Methylglyoxal is a ubiquitous 2-oxoaldehyde derived from glycolysis. Previously, we have reported that methylglyoxal attenuates the rate of overall protein synthesis in Saccharomyces cerevisiae through phosphorylation of the α subunit of translation initiation factor 2 (eIF2α) in a Gcn2-dependent manner. Phosphorylation of eIF2α impedes the formation of a translation initiation complex, and subsequently, overall protein synthesis is reduced. Uncharged tRNA plays an important role in the activation of Gcn2, although we found that MG treatment did not elevate the levels of uncharged tRNA. Rapamycin, a potent inhibitor of TOR kinase, is known to induce phosphorylation of eIF2α without affecting the levels of uncharged tRNA. We determined the correlation between methylglyoxal and TOR kinase activity and found that phosphorylation of eIF2α by methylglyoxal occurred independently of the target of rapamycin (TOR) pathway.
- Subjects
RAPAMYCIN; GLYCOLYSIS; PROTEIN synthesis; SACCHAROMYCES cerevisiae; PHOSPHORYLATION; TRANSFER RNA; SACCHAROMYCES; CHEMICAL reactions; IMMUNOSUPPRESSIVE agents; MICROBIOLOGY
- Publication
Applied Microbiology & Biotechnology, 2010, Vol 86, Issue 6, p1887
- ISSN
0175-7598
- Publication type
Article
- DOI
10.1007/s00253-009-2411-z