In Bacillus subtilis, the Sirtuin Protein Deacetylase, Encoded by the srtN Gene (Formerly yhdZ), and Functions Encoded by the acuABC Genes Control the Activity of Acetyl Coenzyme A Synthetase

In Bacillus subtilis, the Sirtuin Protein Deacetylase, Encoded by the srtN Gene (Formerly yhdZ), and Functions Encoded by the acuABC Genes Control the Activity of Acetyl Coenzyme A Synthetase
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DOI:
10.1128/jb.01674-08
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发表时间:
2009-03-15
影响因子:
3.2
通讯作者:
Escalante-Semerena, Jorge C.
Escalante-Semerena, Jorge C.
中科院分区:
生物学3区
文献类型:
--
作者:
Gardner, Jeffrey G.;Escalante-Semerena, Jorge C.

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本报告提供了在体内的证据的acuA和acuC基因产物的乙酰辅酶A(Ac-CoA)合成酶(阿克萨)的枯草芽孢杆菌的翻译后控制。此外,体内和体外实验数据均支持B.枯草芽孢杆菌编码与酵母Sir 2蛋白(也称为sirtuin)同源的NAD(+)依赖性蛋白脱乙酰酶。在此新信息的基础上,基因命名的变化,从yhdZ srtN(沉默调节蛋白),提出了反映与YdhZ蛋白的活性。B的体内对照。Subtilis阿克萨功能需要AcuC和SrtN的组合活性。acuC或srtN的失活导致在低乙酸条件下比野生型菌株的生长和细胞产率更慢,并且acuC srtN菌株在低乙酸条件下生长与阿克萨菌株一样差。我们对后一结果的解释是,需要两种脱乙酰酶(AcuC和SrtN)来维持阿克萨的活性(即,脱乙酰化),因此细胞可以在低浓度的乙酸盐下生长。acuA acuC srtN菌株在乙酸盐上的生长优于acuA(+)acuC srtN菌株,表明AcuA乙酰转移酶修饰(即,灭活)阿克萨在体内,结果与以前报道的体外证据一致,AcsA是AcuA的底物。
This report provides in vivo evidence for the posttranslational control of the acetyl coenzyme A (Ac-CoA) synthetase (AcsA) enzyme of Bacillus subtilis by the acuA and acuC gene products. In addition, both in vivo and in vitro data presented support the conclusion that the yhdZ gene of B. subtilis encodes a NAD(+)-dependent protein deacetylase homologous to the yeast Sir2 protein (also known as sirtuin). On the basis of this new information, a change in gene nomenclature, from yhdZ to srtN (for sirtuin), is proposed to reflect the activity associated with the YdhZ protein. In vivo control of B. subtilis AcsA function required the combined activities of AcuC and SrtN. Inactivation of acuC or srtN resulted in slower growth and cell yield under low-acetate conditions than those of the wild-type strain, and the acuC srtN strain grew under low-acetate conditions as poorly as the acsA strain. Our interpretation of the latter result was that both deacetylases (AcuC and SrtN) are needed to maintain AcsA as active (i.e., deacetylated) so the cell can grow with low concentrations of acetate. Growth of an acuA acuC srtN strain on acetate was improved over that of the acuA(+) acuC srtN strain, indicating that the AcuA acetyltransferase enzyme modifies (i.e., inactivates) AcsA in vivo, a result consistent with previously reported in vitro evidence that AcsA is a substrate of AcuA.