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首页> 外文期刊>Applied Microbiology >Conserved Pyridoxal 5'-Phosphate-Binding Protein YggS Impacts Amino Acid Metabolism through Pyridoxine 5'-Phosphate in Escherichia coli
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Conserved Pyridoxal 5'-Phosphate-Binding Protein YggS Impacts Amino Acid Metabolism through Pyridoxine 5'-Phosphate in Escherichia coli

机译：保守的吡rid醛5'-磷酸盐结合蛋白YggS通过吡rid醇5'-磷酸盐在大肠杆菌中影响氨基酸代谢。

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Escherichia coli YggS (COG0325) is a member of the highly conserved pyridoxal 5′-phosphate (PLP)-binding protein (PLPBP) family. Recent studies suggested a role for this protein family in the homeostasis of vitamin B6 and amino acids. The deletion or mutation of a member of this protein family causes pleiotropic effects in many organisms and is causative of vitamin B6-dependent epilepsy in humans. To date, little has been known about the mechanism by which lack of YggS results in these diverse phenotypes. In this study, we determined that the pyridoxine (PN) sensitivity observed in yggS-deficient E. coli was caused by the pyridoxine 5′-phosphate (PNP)-dependent overproduction of Val, which is toxic to E. coli. The data suggest that the yggS mutation impacts Val accumulation by perturbing the biosynthetic of Thr from homoserine (Hse). Exogenous Hse inhibited the growth of the yggS mutant, caused further accumulation of PNP, and increased the levels of some intermediates in the Thr-Ile-Val metabolic pathways. Blocking the Thr biosynthetic pathway or decreasing the intracellular PNP levels abolished the perturbations of amino acid metabolism caused by the exogenous PN and Hse. Our data showed that a high concentration of intracellular PNP is the root cause of at least some of the pleiotropic phenotypes described for a yggS mutant of E. coli.IMPORTANCE Recent studies showed that deletion or mutation of members of the YggS protein family causes pleiotropic effects in many organisms. Little is known about the causes, mechanisms, and consequences of these diverse phenotypes. It was previously shown that yggS mutations in E. coli result in the accumulation of PNP and some metabolites in the Ile/Val biosynthetic pathway. This work revealed that some exogenous stresses increase the aberrant accumulation of PNP in the yggS mutant. In addition, the current report provides evidence indicating that some, but not all, of the phenotypes of the yggS mutant in E. coli are due to the elevated PNP level. These results will contribute to continuing efforts to determine the molecular functions of the members of the YggS protein family.
机译：大肠杆菌YggS（COG0325）是高度保守的吡ido醛5'-磷酸（PLP）结合蛋白（PLPBP）家族的成员。最近的研究表明该蛋白家族在维生素B6和氨基酸的体内平衡中起着作用。该蛋白质家族成员的缺失或突变在许多生物中引起多效性作用，并且是人类维生素B6依赖型癫痫的病因。迄今为止，关于YggS缺乏导致这些不同表型的机制还知之甚少。在这项研究中，我们确定在yggS缺陷型大肠杆菌中观察到的吡ido醇（PN）敏感性是由吡ido醇5'-磷酸（PNP）依赖性的Val过量生产引起的，Val对大肠杆菌有毒。数据表明，yggS突变会干扰高丝氨酸（Hse）的Thr的生物合成，从而影响Val的积累。外源Hse抑制了yggS突变体的生长，引起PNP的进一步积累，并增加了Thr-Ile-Val代谢途径中某些中间体的水平。阻断Thr生物合成途径或降低细胞内PNP水平消除了外源PN和Hse引起的氨基酸代谢扰动。我们的数据表明，高浓度的细胞内PNP是大肠杆菌yggS突变体描述的至少一些多效性表型的根本原因。最新研究表明，YggS蛋白家族成员的缺失或突变会引起多效性效应在许多生物中。这些不同的表型的原因，机制和后果知之甚少。先前已证明，大肠杆菌中的yggS突变导致Ple的积累和Ile / Val生物合成途径中的某些代谢产物。这项工作表明，一些外源压力会增加yggS突变体中PNP的异常积累。此外，本报告提供的证据表明，大肠杆菌中yggS突变体的某些而非全部表型是由于PNP水平升高所致。这些结果将有助于确定YggS蛋白家族成员的分子功能的不断努力。

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