| Integration of general amino acid control and target of rapamycin (TOR) regulatory pathways in nitrogen assimilation in yeast. | |
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MedLine Citation:
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PMID: 20233714 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Two important nutrient-sensing and regulatory pathways, the general amino acid control (GAAC) and the target of rapamycin (TOR), participate in the control of yeast growth and metabolism during changes in nutrient availability. Amino acid starvation activates the GAAC through Gcn2p phosphorylation of translation factor eIF2 and preferential translation of GCN4, a transcription activator. TOR senses nitrogen availability and regulates transcription factors such as Gln3p. We used microarray analyses to address the integration of the GAAC and TOR pathways in directing the yeast transcriptome during amino acid starvation and rapamycin treatment. We found that GAAC is a major effector of the TOR pathway, with Gcn4p and Gln3p each inducing a similar number of genes during rapamycin treatment. Although Gcn4p activates a common core of 57 genes, the GAAC directs significant variations in the transcriptome during different stresses. In addition to inducing amino acid biosynthetic genes, Gcn4p in conjunction with Gln3p activates genes required for the assimilation of secondary nitrogen sources such as gamma-aminobutyric acid (GABA). Gcn2p activation upon shifting to secondary nitrogen sources is suggested to occur by means of a dual mechanism. First, Gcn2p is induced by the release of TOR repression through a mechanism involving Sit4p protein phosphatase. Second, this eIF2 kinase is activated by select uncharged tRNAs, which were shown to accumulate during the shift to the GABA medium. This study highlights the mechanisms by which the GAAC and TOR pathways are integrated to recognize changing nitrogen availability and direct the transcriptome for optimal growth adaptation. |
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Authors:
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Kirk A Staschke; Souvik Dey; John M Zaborske; Lakshmi Reddy Palam; Jeanette N McClintick; Tao Pan; Howard J Edenberg; Ronald C Wek |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2010-03-16 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 285 ISSN: 1083-351X ISO Abbreviation: J. Biol. Chem. Publication Date: 2010 May |
Date Detail:
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Created Date: 2010-05-24 Completed Date: 2010-06-17 Revised Date: 2011-07-28 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 16893-911 Citation Subset: IM |
Affiliation:
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Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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chemistry* Gene Expression Profiling Gene Expression Regulation* Intracellular Signaling Peptides and Proteins / physiology* Models, Biological Nitrogen / chemistry* Phosphorylation Protein Biosynthesis Protein Phosphatase 2 / metabolism Protein-Serine-Threonine Kinases / metabolism, physiology* RNA, Transfer / chemistry Saccharomyces cerevisiae / metabolism* Saccharomyces cerevisiae Proteins / metabolism Species Specificity TOR Serine-Threonine Kinases Transcription, Genetic gamma-Aminobutyric Acid / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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R01GM49164/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Intracellular Signaling Peptides and Proteins; 0/Saccharomyces cerevisiae Proteins; 56-12-2/gamma-Aminobutyric Acid; 7727-37-9/Nitrogen; 9014-25-9/RNA, Transfer; EC 2.7.1.1/TOR Serine-Threonine Kinases; EC 2.7.11.1/GCN2 protein, S cerevisiae; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 3.1.3.16/Protein Phosphatase 2; EC 3.1.3.16/SIT4 protein, S cerevisiae |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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