The roles of stress-activated Sty1 and Gcn2 kinases and of the protooncoprotein homologue Int6/eIF3e in responses to endogenous oxidative stress during histidine starvation.
Authors
Nemoto, NUdagawa, T
Ohira, T
Jiang, L
Hirota, K
Wilkinson, Caroline R M
Bähler, J
Jones, Nic
Ohta, K
Wek, R
Asano, K
Affiliation
Molecular, Cellular, and Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.Issue Date
2010-11-26
Metadata
Show full item recordAbstract
In fission yeast, Sty1 and Gcn2 are important protein kinases that regulate gene expression in response to amino acid starvation. The translation factor subunit Int6/eIF3e promotes Sty1-dependent response by increasing the abundance of Atf1, a transcription factor targeted by Sty1. While Gcn2 promotes expression of amino acid biosynthesis enzymes, the mechanism and function of Sty1 activation and Int6/eIF3e involvement during this nutrient stress are not understood. Here we show that mutants lacking sty1(+) or gcn2(+) display reduced viabilities during histidine depletion stress in a manner suppressible by the antioxidant N-acetyl cysteine, suggesting that these protein kinases function to alleviate endogenous oxidative damage generated during nutrient starvation. Int6/eIF3e also promotes cell viability by a mechanism involving the stimulation of Sty1 response to oxidative damage. In further support of these observations, microarray data suggest that, during histidine starvation, int6Δ increases the duration of Sty1-activated gene expression linked to oxidative stress due to the initial attenuation of Sty1-dependent transcription. Moreover, loss of gcn2 induces the expression of a new set of genes not activated in wild-type cells starved for histidine. These genes encode heatshock proteins, redox enzymes, and proteins involved in mitochondrial maintenance, in agreement with the idea that oxidative stress is imposed on gcn2Δ cells. Furthermore, early Sty1 activation promotes rapid Gcn2 activation on histidine starvation. These results suggest that Gcn2, Sty1, and Int6/eIF3e are functionally integrated and cooperate to respond to oxidative stress generated during histidine starvation.Citation
The roles of stress-activated Sty1 and Gcn2 kinases and of the protooncoprotein homologue Int6/eIF3e in responses to endogenous oxidative stress during histidine starvation. 2010, 404 (2):183-201 J Mol BiolJournal
Journal of Molecular BiologyDOI
10.1016/j.jmb.2010.09.016PubMed ID
20875427Type
ArticleLanguage
enISSN
1089-8638ae974a485f413a2113503eed53cd6c53
10.1016/j.jmb.2010.09.016
Scopus Count
Collections
Related articles
- Int6/eIF3e promotes general translation and Atf1 abundance to modulate Sty1 MAPK-dependent stress response in fission yeast.
- Authors: Udagawa T, Nemoto N, Wilkinson CR, Narashimhan J, Jiang L, Watt S, Zook A, Jones N, Wek RC, Bähler J, Asano K
- Issue date: 2008 Aug 8
- Deciphering the role of the signal- and Sty1 kinase-dependent phosphorylation of the stress-responsive transcription factor Atf1 on gene activation.
- Authors: Salat-Canela C, Paulo E, Sánchez-Mir L, Carmona M, Ayté J, Oliva B, Hidalgo E
- Issue date: 2017 Aug 18
- Role of mitogen-activated protein kinase Sty1 in regulation of eukaryotic initiation factor 2alpha kinases in response to environmental stress in Schizosaccharomyces pombe.
- Authors: Berlanga JJ, Rivero D, Martín R, Herrero S, Moreno S, de Haro C
- Issue date: 2010 Jan
- Phosphorylation of the Transcription Factor Atf1 at Multiple Sites by the MAP Kinase Sty1 Controls Homologous Recombination and Transcription.
- Authors: Sánchez-Mir L, Fraile R, Ayté J, Hidalgo E
- Issue date: 2020 Sep 4
- Transcription factors Atf1 and Sty1 promote stress tolerance under nitrosative stress in Schizosaccharomyces pombe.
- Authors: Kar P, Biswas P, Patra SK, Ghosh S
- Issue date: 2018 Jan