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Microbiology 146 (2000), 2113-2120
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Microbiology (2000), 146, 2113-2120.
© 2000 Society for General Microbiology


Physiology and Growth

Hyperphosphorylation of Msn2p and Msn4p in response to heat shock and the diauxic shift is inhibited by cAMP in Saccharomyces cerevisiae

Hervé Garreau1, Rukhsana Nilofer Hasan1, Georges Renault1, Francisco Estruch2, Emmanuelle Boy-Marcotte1 and Michel Jacquet1

Laboratoire Information Génétique et Développement, Institut de Génétique et Microbiologie, UMR CNRS C8621, Université Paris-Sud, Bâtiment 400, 91405 Orsay cedex, France1
Dpto. Bioquímica y Biol. Molecular, Universitat de Valencia, and Dpto. Biotecnologia IATA, CSIC, Apdo Correos 73.46100 Burjassot, Valencia, Spain2

Author for correspondence: Hervé Garreau. Tel: +33 1 69 15 46 30. Fax: +33 1 69 15 72 96. e-mail: garreau{at}igmors.u-psud.fr

In response to various stresses, as well as during the diauxic transition, the Msn2p and Msn4p transcription factors of Saccharomyces cerevisiae are activated and induce a large set of genes. This activation is inhibited by the Ras/cAMP/PKA (cAMP-dependent protein kinase) pathway. Here we show by immunoblotting experiments that Msn2p and Msn4p are phosphorylated in vivo during growth on glucose, and become hyperphosphorylated at the diauxic transition and upon heat shock. This hyperphosphorylation is correlated with activation of Msn2/4p-dependent transcription. An increased level of cAMP prevents and reverses these hyperphosphorylations, indicating that kinases other than PKA are involved. These results suggest that PKA and stress-activated kinases control Msn2/4p activity by antagonistic phosphorylation. It was also noted that Msn4p is transiently increased at the diauxic transition. Msn2p and Msn4p present different hyperphosphorylation patterns in response to different stresses.

Keywords: Saccharomyces cerevisiae, stress response, transcription factor, cAMP-dependent protein kinase

Abbreviations: PKA, cAMP-dependent protein kinase; STRE, stress-response element




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