Downloads: 342

Files in This Item:
File Description SizeFormat 
Inoue_2010_AMB.pdf279.48 kBAdobe PDFView/Open
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
TORC1
Gcn2
eIF2α
S. cerevisiae
Rapamycin
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 www.springerlink.com
This is not the published version. Please cite only the published version.
この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
URI: http://hdl.handle.net/2433/123517
DOI(Published Version): 10.1007/s00253-009-2411-z
PubMed ID: 20077113
Appears in Collections:Journal Articles

Show full item record

Export to RefWorks


Export Format: 


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.