Document Detail


Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway.
MedLine Citation:
PMID:  16407266     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We have identified carbon catabolite repression (CCR) as a regulator of amino acid permeases in Saccharomyces cerevisiae, elucidated the permeases regulated by CCR, and identified the mechanisms involved in amino acid permease regulation by CCR. Transport of l-arginine and l-leucine was increased by approximately 10-25-fold in yeast grown in carbon sources alternate to glucose, indicating regulation by CCR. In wild type yeast the uptake (pmol/10(6) cells/h), in glucose versus galactose medium, of l-[(14)C]arginine was (0.24 +/- 0.04 versus 6.11 +/- 0.42) and l-[(14)C]leucine was (0.30 +/- 0.02 versus 3.60 +/- 0.50). The increase in amino acid uptake was maintained when galactose was replaced with glycerol. Deletion of gap1Delta and agp1Delta from the wild type strain did not alter CCR induced increase in l-leucine uptake; however, deletion of further amino acid permeases reduced the increase in l-leucine uptake in the following manner: 36% (gnp1Delta), 62% (bap2Delta), 83% (Delta(bap2-tat1)). Direct immunofluorescence showed large increases in the expression of Gnp1 and Bap2 proteins when grown in galactose compared with glucose medium. By extending the functional genomic approach to include major nutritional transducers of CCR in yeast, we concluded that SNF/MIG, GCN, or PSK pathways were not involved in the regulation of amino acid permeases by CCR. Strikingly, the deletion of TOR1, which regulates cellular response to changes in nitrogen availability, from the wild type strain abolished the CCR-induced amino acid uptake. Our results provide novel insights into the regulation of yeast amino acid permeases and signaling mechanisms involved in this regulation.
Authors:
George J Peter; Louis Düring; Aamir Ahmed
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-01-04
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  281     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-02-27     Completed Date:  2006-05-23     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5546-52     Citation Subset:  IM    
Affiliation:
Institute of Urology and Nephrology, University College London, 67 Riding House Street, London W1W 7EY, United Kingdom.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Transport Systems / metabolism*
Amino Acids / chemistry,  metabolism
Culture Media / chemistry
DNA-Binding Proteins / metabolism*
Fungal Proteins / metabolism*
Protein-Serine-Threonine Kinases
Recombinant Fusion Proteins / genetics,  metabolism
Repressor Proteins / metabolism*
Saccharomyces cerevisiae / genetics,  metabolism*
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Signal Transduction / physiology*
Grant Support
ID/Acronym/Agency:
//Wellcome Trust
Chemical
Reg. No./Substance:
0/Amino Acid Transport Systems; 0/Amino Acids; 0/Culture Media; 0/DNA-Binding Proteins; 0/Fungal Proteins; 0/Recombinant Fusion Proteins; 0/Repressor Proteins; 0/Saccharomyces cerevisiae Proteins; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/target of rapamycin protein, S cerevisiae

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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