CobB1 deacetylase activity in Streptomyces coelicolor
| Autor: | Eva Stodůlková, Eva Kudrnáčová, Vaclav Zidek, Silvia Bezoušková, Jarmila Zídková, Karel Mikulík, Dita Setinová, Jürgen Felsberg |
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| Rok vydání: | 2012 |
| Předmět: |
Transcription
Genetic Molecular Sequence Data Acetate-CoA Ligase Anthraquinones Streptomyces coelicolor Biochemistry chemistry.chemical_compound Bacterial Proteins Catalytic Domain Sirtuins Amino Acid Sequence Bovine serum albumin Enzyme Inhibitors Molecular Biology Conserved Sequence chemistry.chemical_classification biology Nicotinamide digestive oral and skin physiology Acetylation Cell Biology Gene Expression Regulation Bacterial biology.organism_classification Molecular biology Recombinant Proteins Enzyme chemistry Sirtuin biology.protein NAD+ kinase Protein Processing Post-Translational Sequence Alignment Deacetylase activity |
| Zdroj: | Biochemistry and cell biology = Biochimie et biologie cellulaire. 90(2) |
| ISSN: | 1208-6002 |
| Popis: | Silent information regulators are NAD+-dependent enzymes that display differential specificity toward acetylated substrates. This report provides first evidence for deacetylation activity of CobB1 in Streptomyces coelicolor. The protein is highly conserved in streptomycetes. The CobB1 protein catalytically removes the acetyl group from acetylated bovine serum albumin. In the absence of NAD+ or when NAD+ was substituted with nicotinamide, deacetylation was stopped. We isolated gene encoding AcetylCoA synthetaseA. The recombinant enzyme produces Acetyl-CoA from acetate. The highest acsA-mRNA level was detected in cells from the exponential phase of growth, and then decreased in transition and stationary phases of growth. Acetylated acsA loses the ability to transfer acetate to CoA. Deacetylation of the enzyme required CobB1, ATP-Mg2, and NAD+. Using specific antibodies against acetylated lys, CobB1, and acsA, we found relationship between level of CobB1 and acetylation of acsA, indicating that CobB1 is involved in regulating the acetylation level of acsA and consequently its activity. It was found that 1-acetyl-tetrahydroxy and 1-acetyl pentahydroxy antraquinone inhibit the deacetylation activity of CobB1. |
| Databáze: | OpenAIRE |
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