Access count of this item: 442

Files in This Item:
File Description SizeFormat 
Inoue_2010_BJ_Table.pdf23.44 kBAdobe PDFView/Open
Inoue_2010_BJ_Suppl Fig .pdf844.1 kBAdobe PDFView/Open
Inoue_2010_BJ_Figs.pdf4.69 MBAdobe PDFView/Open
Inoue_2010_BJ.pdf340.49 kBAdobe PDFView/Open
Title: Calcineurin/Crz1 destabilizes Msn2 and Msn4 in the nucleus in response to Ca(2+) in Saccharomyces cerevisiae.
Authors: Takatsume, Yoshifumi
Ohdate, Takumi
Maeta, Kazuhiro
Nomura, Wataru
Izawa, Shingo
Inoue, Yoshiharu  kyouindb  KAKEN_id
Author's alias: 井上, 善晴
Keywords: calcineurin
calcium
Crz1
FK506
methylglyoxal
Msn2/Msn4
Issue Date: 15-Apr-2010
Publisher: Portland Press
Journal title: The Biochemical journal
Volume: 427
Issue: 2
Start page: 275
End page: 287
Abstract: Although methylglyoxal is derived from glycolysis, it has adverse effects on cellular function. Hence, the intrinsic role of methylglyoxal in vivo remains to be determined. Glyoxalase 1 is a pivotal enzyme in the metabolism of methylglyoxal in all types of organisms. To learn about the physiological roles of methylglyoxal, we have screened conditions that alter the expression of the gene encoding glyoxalase 1, GLO1, in Saccharomyces cerevisiae. We show that the expression of GLO1 is induced following treatment with Ca2+ and is dependent on the MAPK (mitogen-activated protein kinase) Hog1 protein and the Msn2/Msn4 transcription factors. Intriguingly, the Ca2+-induced expression of GLO1 was enhanced in the presence of FK506, a potent inhibitor of calcineurin. Consequently, the Ca2+-induced expression of GLO1 in a mutant that is defective in calcineurin or Crz1, the sole transcription factor downstream of calcineurin, was much greater than that in the wild-type strain even without FK506. This phenomenon was dependent upon a cis-element, the STRE (stress-response element), in the promoter that is able to mediate the response to Ca2+ signalling together with Hog1 and Msn2/Msn4. The level of Ca2+-induced expression of GLO1 reached a maximum in cells overexpressing MSN2 even when FK506 was not present, whereas in cells overexpressing CRZ1 the level was greatly reduced and increased markedly when FK506 was present. We also found that the levels of Msn2 and Msn4 proteins in Ca2+-treated cells decreased gradually and that FK506 blocked the degradation of Msn2/Msn4. We propose that Crz1 destabilizes Msn2/Msn4 in the nuclei of cells in response to Ca2+ signalling.
Rights: © The Authors Journal compilation © 2010 Biochemical Society
The Version of Record (VoR) is available at www.biochemj.org
許諾条件により本文は2010-10-15に公開.
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/2433/123771
DOI(Published Version): 10.1042/BJ20091334
PubMed ID: 20121702
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.