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Title: Methylglyoxal activates Gcn2 to phosphorylate eIF2α independently of the TOR pathway in Saccharomyces cerevisiae.
Authors: Nomura, Wataru  kyouindb  KAKEN_id
Maeta, Kazuhiro
Kita, Keiko  kyouindb  KAKEN_id
Izawa, Shingo
Inoue, Yoshiharu  kyouindb  KAKEN_id
Author's alias: 井上, 善晴
Keywords: Methylglyoxal
S. cerevisiae
Issue Date: May-2010
Publisher: Springer
Journal title: Applied microbiology and biotechnology
Volume: 86
Issue: 6
Start page: 1887
End page: 1894
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 alpha subunit of translation initiation factor 2 (eIF2alpha) in a Gcn2-dependent manner. Phosphorylation of eIF2alpha 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 eIF2alpha without affecting the levels of uncharged tRNA. We determined the correlation between methylglyoxal and TOR kinase activity and found that phosphorylation of eIF2alpha by methylglyoxal occurred independently of the target of rapamycin (TOR) pathway.
Rights: The original publication is available at
This is not the published version. Please cite only the published version.
DOI(Published Version): 10.1007/s00253-009-2411-z
PubMed ID: 20077113
Appears in Collections:Journal Articles

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