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Studying the Lysine Acetylation of Malate Dehydrogenase.
Venkat, Sumana; Gregory, Caroline; Sturges, Jourdan; Gan, Qinglei; Fan, Chenguang.
Afiliación
  • Venkat S; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA; Cell and Molecular Biology Program, University of Arkansas, Fayetteville, AR 72701, USA.
  • Gregory C; Department of Biological Sciences, University of Arkansas, Fayetteville, AR 72701, USA.
  • Sturges J; Department of Biological Sciences, University of Arkansas, Fayetteville, AR 72701, USA.
  • Gan Q; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA.
  • Fan C; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA; Cell and Molecular Biology Program, University of Arkansas, Fayetteville, AR 72701, USA. Electronic address: cf021@uark.edu.
J Mol Biol ; 429(9): 1396-1405, 2017 05 05.
Article en En | MEDLINE | ID: mdl-28366830
Protein acetylation plays important roles in many biological processes. Malate dehydrogenase (MDH), a key enzyme in the tricarboxylic acid cycle, has been identified to be acetylated in bacteria by proteomic studies, but no further characterization has been reported. One challenge for studying protein acetylation is to get purely acetylated proteins at specific positions. Here, we applied the genetic code expansion strategy to site-specifically incorporate Nε-acetyllysine into MDH. The acetylation of lysine residues in MDH could enhance its enzyme activity. The Escherichia coli deacetylase CobB could deacetylate acetylated MDH, while the E. coli acetyltransferase YfiQ cannot acetylate MDH efficiently. Our results also demonstrated that acetyl-CoA or acetyl-phosphate could acetylate MDH chemically in vitro. Furthermore, the acetylation level of MDH was shown to be affected by carbon sources in the growth medium.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Escherichia coli / Lisina / Malato Deshidrogenasa Idioma: En Revista: J Mol Biol Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Escherichia coli / Lisina / Malato Deshidrogenasa Idioma: En Revista: J Mol Biol Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos