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    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.

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    Authors
    Nemoto, N
    Udagawa, T
    Ohira, T
    Jiang, L
    Hirota, K
    Wilkinson, Caroline R M
    Bähler, J
    Jones, Nic
    Ohta, K
    Wek, R
    Asano, K
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    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 record
    Abstract
    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 Biol
    Journal
    Journal of Molecular Biology
    URI
    http://hdl.handle.net/10541/120267
    DOI
    10.1016/j.jmb.2010.09.016
    PubMed ID
    20875427
    Type
    Article
    Language
    en
    ISSN
    1089-8638
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.jmb.2010.09.016
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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