Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae.
Genetics
; 163(2): 545-55, 2003 Feb.
Article
em En
| MEDLINE
| ID: mdl-12618394
ABSTRACT
SIR2 proteins have NAD(+)-dependent histone deacetylase activity, but no metabolic role has been assigned to any of these proteins. In Salmonella enterica, SIR2 function was required for activity of the acetyl-CoA synthetase (Acs) enzyme. A greater than two orders of magnitude increase in the specific activity of Acs enzyme synthesized by a sirtuin-deficient strain was measured after treatment with homogeneous S. enterica SIR2 protein. Human SIR2A and yeast SIR2 proteins restored growth of SIR2-deficient S. enterica on acetate and propionate, suggesting that eukaryotic cells may also use SIR2 proteins to control the synthesis of acetyl-CoA by the level of acetylation of acetyl-CoA synthetases. Consistent with this idea, growth of a quintuple sir2 hst1 hst2 hst3 hst4 mutant strain of the yeast Saccharomyces cerevisiae on acetate or propionate was severely impaired. The data suggest that the Hst3 and Hst4 proteins are the most important for allowing growth on these short-chain fatty acids.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Coenzima A Ligases
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Salmonella enterica
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Proteínas de Escherichia coli
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Sirtuínas
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Proteínas Reguladoras de Informação Silenciosa de Saccharomyces cerevisiae
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Ácidos Graxos
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Histona Desacetilases
Idioma:
En
Revista:
Genetics
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Estados Unidos