Document Detail


The SAGA histone acetyltransferase complex regulates leucine uptake through the Agp3 permease in fission yeast.
MedLine Citation:
PMID:  22992726     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Metabolic responses of unicellular organisms are mostly acute, transient, and cell-autonomous. Regulation of nutrient uptake in yeast is one such rapid response. High quality nitrogen sources such as NH(4)(+) inhibit uptake of poor nitrogen sources, such as amino acids. Both transcriptional and posttranscriptional mechanisms operate in nutrient uptake regulation; however, many components of this system remain uncharacterized in the fission yeast, Schizosaccharomyces pombe. Here, we demonstrate that the Spt-Ada-Gcn acetyltransferase (SAGA) complex modulates leucine uptake. Initially, we noticed that a branched-chain amino acid auxotroph exhibits a peculiar adaptive growth phenotype on solid minimal media containing certain nitrogen sources. In fact, the growth of many auxotrophic strains is inhibited by excess NH(4)Cl, possibly through nitrogen-mediated uptake inhibition of the corresponding nutrients. Surprisingly, DNA microarray analysis revealed that the transcriptional reprogramming during the adaptation of the branched-chain amino acid auxotroph was highly correlated with reprogramming observed in deletions of the SAGA histone acetyltransferase module genes. Deletion of gcn5(+) increased leucine uptake in the prototrophic background and rendered the leucine auxotroph resistant to NH(4)Cl. Deletion of tra1(+) caused the opposite phenotypes. The increase in leucine uptake in the gcn5Δ mutant was dependent on an amino acid permease gene, SPCC965.11c(+). The closest budding yeast homolog of this permease is a relatively nonspecific amino acid permease AGP3, which functions in poor nutrient conditions. Our analysis identified the regulation of nutrient uptake as a physiological function for the SAGA complex, providing a potential link between cellular metabolism and chromatin regulation.
Authors:
Hidekazu Takahashi; Xiaoying Sun; Makiko Hamamoto; Yoko Yashiroda; Minoru Yoshida
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-09-18
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  287     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-05     Completed Date:  2013-01-23     Revised Date:  2013-11-05    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  38158-67     Citation Subset:  IM    
Affiliation:
Chemical Genetics Laboratory/Chemical Genomics Research Group, RIKEN Advanced Science Institute, Wako, Saitama 351-0198, Japan.
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MeSH Terms
Descriptor/Qualifier:
Acetyltransferases / genetics,  metabolism*
Amino Acid Transport Systems / genetics,  metabolism*
Amino Acids / metabolism,  pharmacology
Ammonium Chloride / pharmacology
Biological Transport / drug effects
Culture Media / pharmacology
Gene Expression Profiling
Leucine / metabolism,  pharmacology
Mutation
Oligonucleotide Array Sequence Analysis
Schizosaccharomyces / genetics,  growth & development,  metabolism*
Schizosaccharomyces pombe Proteins / genetics,  metabolism*
Transaminases / genetics,  metabolism
Chemical
Reg. No./Substance:
0/Amino Acid Transport Systems; 0/Amino Acids; 0/Culture Media; 0/SPCC965.11c protein, S pombe; 0/Schizosaccharomyces pombe Proteins; 12125-02-9/Ammonium Chloride; 61-90-5/Leucine; EC 2.3.1.-/Acetyltransferases; EC 2.3.1.48/Gcn5 protein, S pombe; EC 2.6.1.-/Transaminases; EC 2.6.1.42/branched-chain-amino-acid transaminase
Comments/Corrections

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