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dc.contributor.authorReiter, Wolfgang
dc.contributor.authorWatt, Stephen
dc.contributor.authorDawson, Keren
dc.contributor.authorLawrence, Clare L
dc.contributor.authorBähler, Jürg
dc.contributor.authorJones, Nic
dc.contributor.authorWilkinson, Caroline R M
dc.date.accessioned2009-04-01T23:26:36Z
dc.date.available2009-04-01T23:26:36Z
dc.date.issued2008-04-11
dc.identifier.citationFission yeast MAP kinase Sty1 is recruited to stress-induced genes. 2008, 283 (15):9945-56 J. Biol. Chem.en
dc.identifier.issn0021-9258
dc.identifier.pmid18252721
dc.identifier.doi10.1074/jbc.M710428200
dc.identifier.urihttp://hdl.handle.net/10541/58733
dc.description.abstractThe stress-induced expression of many fission yeast genes is dependent upon the Sty1 mitogen-activated protein kinase (MAPK) and Atf1 transcription factor. Atf1 is phosphorylated by Sty1 yet this phosphorylation is not required for stress-induced gene expression, suggesting another mechanism exists whereby Sty1 activates transcription. Here we show that Sty1 associates with Atf1-dependent genes and is recruited to both their promoters and coding regions. This occurs in response to various stress conditions coincident with the kinetics of the activation of Sty1. Association with promoters is not a consequence of increased nuclear accumulation of Sty1 nor does it require the phosphorylation of Atf1. However, recruitment is completely abolished in a mutant lacking Sty1 kinase activity. Both Atf1 and its binding partner Pcr1 are required for association of Sty1 with Atf1-dependent promoters, suggesting that this heterodimer must be intact for optimal recruitment of the MAPK. However, many Atf1-dependent genes are still expressed in a pcr1Delta mutant but with significantly delayed kinetics, thus providing an explanation for the relatively mild stress sensitivity displayed by pcr1Delta. Consistent with this delay, Sty1 and Atf1 cannot be detected at these promoters in this condition, suggesting that their association with chromatin is weak or transient in the absence of Pcr1.
dc.language.isoenen
dc.subjectFission Yeasten
dc.subjectSty1en
dc.subject.meshActivating Transcription Factor 1
dc.subject.meshActivating Transcription Factors
dc.subject.meshActive Transport, Cell Nucleus
dc.subject.meshCell Nucleus
dc.subject.meshChromatin
dc.subject.meshGene Deletion
dc.subject.meshGene Expression Regulation, Fungal
dc.subject.meshMitogen-Activated Protein Kinases
dc.subject.meshOpen Reading Frames
dc.subject.meshPhosphoproteins
dc.subject.meshPhosphorylation
dc.subject.meshPromoter Regions, Genetic
dc.subject.meshSchizosaccharomyces
dc.subject.meshSchizosaccharomyces Pombe Proteins
dc.titleFission yeast MAP kinase Sty1 is recruited to stress-induced genes.en
dc.typeArticleen
dc.contributor.departmentPaterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester, UK.en
dc.identifier.journalThe Journal of Biological Chemistryen
html.description.abstractThe stress-induced expression of many fission yeast genes is dependent upon the Sty1 mitogen-activated protein kinase (MAPK) and Atf1 transcription factor. Atf1 is phosphorylated by Sty1 yet this phosphorylation is not required for stress-induced gene expression, suggesting another mechanism exists whereby Sty1 activates transcription. Here we show that Sty1 associates with Atf1-dependent genes and is recruited to both their promoters and coding regions. This occurs in response to various stress conditions coincident with the kinetics of the activation of Sty1. Association with promoters is not a consequence of increased nuclear accumulation of Sty1 nor does it require the phosphorylation of Atf1. However, recruitment is completely abolished in a mutant lacking Sty1 kinase activity. Both Atf1 and its binding partner Pcr1 are required for association of Sty1 with Atf1-dependent promoters, suggesting that this heterodimer must be intact for optimal recruitment of the MAPK. However, many Atf1-dependent genes are still expressed in a pcr1Delta mutant but with significantly delayed kinetics, thus providing an explanation for the relatively mild stress sensitivity displayed by pcr1Delta. Consistent with this delay, Sty1 and Atf1 cannot be detected at these promoters in this condition, suggesting that their association with chromatin is weak or transient in the absence of Pcr1.


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