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dc.contributor.authorLeverentz, Michael K
dc.contributor.authorCampbell, Robert N
dc.contributor.authorConnolly, Yvonne
dc.contributor.authorWhetton, Anthony D
dc.contributor.authorReece, Richard J
dc.date.accessioned2009-12-08T12:16:20Z
dc.date.available2009-12-08T12:16:20Z
dc.date.issued2009-09-04
dc.identifier.citationMutation of a phosphorylatable residue in Put3p affects the magnitude of rapamycin-induced PUT1 activation in a Gat1p-dependent manner. 2009, 284 (36):24115-22 J. Biol. Chem.en
dc.identifier.issn0021-9258
dc.identifier.pmid19574222
dc.identifier.doi10.1074/jbc.M109.030361
dc.identifier.urihttp://hdl.handle.net/10541/87562
dc.description.abstractSaccharomyces cerevisiae can utilize high quality (e.g. glutamine and ammonia) as well as low quality (e.g. gamma-amino butyric acid and proline) nitrogen sources. The transcriptional activator Put3p allows yeast cells to utilize proline as a nitrogen source through expression of the PUT1 and PUT2 genes. Put3p activates high level transcription of these genes by binding proline directly. However, Put3p also responds to other lower quality nitrogen sources. As nitrogen quality decreases, Put3p exhibits an increase in phosphorylation concurrent with an increase in PUT gene expression. The proline-independent activation of the PUT genes requires both Put3p and the positively acting GATA factors, Gln3p and Gat1p. Conversely, the phosphorylation of Put3p is not dependent on GATA factor activity. Here, we find that the mutation of Put3p at amino acid Tyr-788 modulates the proline-independent activation of PUT1 through Gat1p. The phosphorylation of Put3p appears to influence the association of Gat1p, but not Gln3p, to the PUT1 promoter. Combined, our findings suggest that this may represent a mechanism through which yeast cells rapidly adapt to use proline as a nitrogen source under nitrogen limiting conditions.
dc.language.isoenen
dc.subject.meshAntifungal Agents
dc.subject.meshGATA Transcription Factors
dc.subject.meshGene Expression Regulation, Fungal
dc.subject.meshMutation
dc.subject.meshPhosphorylation
dc.subject.meshProline
dc.subject.meshProline Oxidase
dc.subject.meshSaccharomyces cerevisiae
dc.subject.meshSaccharomyces cerevisiae Proteins
dc.subject.meshSirolimus
dc.subject.meshTranscription Factors
dc.subject.meshTranscription, Genetic
dc.titleMutation of a phosphorylatable residue in Put3p affects the magnitude of rapamycin-induced PUT1 activation in a Gat1p-dependent manner.en
dc.typeArticleen
dc.contributor.departmentFaculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, United Kingdom.en
dc.identifier.journalThe Journal of Biological Chemistryen
html.description.abstractSaccharomyces cerevisiae can utilize high quality (e.g. glutamine and ammonia) as well as low quality (e.g. gamma-amino butyric acid and proline) nitrogen sources. The transcriptional activator Put3p allows yeast cells to utilize proline as a nitrogen source through expression of the PUT1 and PUT2 genes. Put3p activates high level transcription of these genes by binding proline directly. However, Put3p also responds to other lower quality nitrogen sources. As nitrogen quality decreases, Put3p exhibits an increase in phosphorylation concurrent with an increase in PUT gene expression. The proline-independent activation of the PUT genes requires both Put3p and the positively acting GATA factors, Gln3p and Gat1p. Conversely, the phosphorylation of Put3p is not dependent on GATA factor activity. Here, we find that the mutation of Put3p at amino acid Tyr-788 modulates the proline-independent activation of PUT1 through Gat1p. The phosphorylation of Put3p appears to influence the association of Gat1p, but not Gln3p, to the PUT1 promoter. Combined, our findings suggest that this may represent a mechanism through which yeast cells rapidly adapt to use proline as a nitrogen source under nitrogen limiting conditions.


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