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Loss of YggS (COG0325) impacts aspartate metabolism in Salmonella enterica
Molecular Microbiology ( IF 3.6 ) Pub Date : 2021-09-08 , DOI: 10.1111/mmi.14810
Huong N Vu 1 , Diana M Downs 1
Affiliation  

YggS is a pyridoxal 5′-phosphate (PLP)-binding protein of the conserved COG0325 family. Despite a connection with vitamin B6 homeostasis in many species, neither a precise biochemical activity nor the molecular mechanism of how YggS contributes to cellular function has been described. In a transposon mutagenesis screen, we found that insertions in aspC (encoding a PLP-dependent aspartate aminotransferase, EC 2.6.1.1) in a Salmonella enterica strain lacking yggS caused a synthetic growth defect, which could be rescued by the addition of exogenous aspartate. Characterization of spontaneous suppressors which improved the growth of the yggS aspC double mutant suggested that this synthetic aspartate limitation was dependent on TyrB, a PLP-dependent aromatic amino acid aminotransferase (EC 2.6.1.57). Genetic and biochemical data were consistent with the hypothesis that TyrB activity was inhibited by accumulated pyridoxine 5′-phosphate and α-keto acids caused by a yggS mutation. This study provides data consistent with a working model implicating YggS in modulating concentrations of B6 vitamers via transamination.

中文翻译:

YggS (COG0325) 的缺失影响肠道沙门氏菌的天冬氨酸代谢

YggS 是保守的 COG0325 家族的 5'-磷酸吡哆醛 (PLP) 结合蛋白。尽管在许多物种中与维生素 B 6稳态有关,但尚未描述 YggS 如何促进细胞功能的精确生化活性和分子机制。在转座子诱变筛选中,我们发现在缺乏yggS的肠沙门氏菌菌株中插入aspC(编码 PLP 依赖性天冬氨酸氨基转移酶,EC 2.6.1.1)会导致合成生长缺陷,这可以通过添加外源天冬氨酸来挽救。改善yggS aspC生长的自发抑制因子的表征双突变体表明这种合成天冬氨酸限制依赖于 TyrB,一种 PLP 依赖性芳香族氨基酸氨基转移酶 (EC 2.6.1.57)。遗传和生化数据与由yggS突变引起的累积的 5'-磷酸吡哆醇和 α-酮酸抑制 TyrB 活性的假设一致。该研究提供的数据与一个工作模型一致,该模型暗示YggS 通过转氨作用调节 B 6维生素的浓度。
更新日期:2021-10-25
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