Post-Transitional Modification: Salmonella PutA Protein

描述(由申请人提供) 沙门氏菌的腐蛋白是一种复杂的多功能蛋白， 与膜结合时，作为黄素脱氢酶起作用，并作为 位于细胞质中的转录抑制因子。此外，Puta是 体内和体内丝氨酸、苏氨酸和酪氨酸残基上的自磷酸化 体外培养。PUTA蛋白含有许多丝氨酸、苏氨酸和酪氨酸残基，以及 丝氨酸、苏氨酸和酪氨酸残基的位置 磷酸化是未知的。此外，虽然已经提出了一种模型， 磷酸化限制了细胞膜中过量粘液的毒性积累， 因为不可能直接测试这一假设，所以函数 PUTA的自磷酸化作用尚不清楚。这项研究的主要目标是 识别Puta中被磷酸化的位置，以构建 改变这些位点的磷酸化的突变，并确定 这些突变对PUTA各功能的影响。此外，这一点 研究将确定Puta蛋白的功能结构域。这些研究可能 揭示了协调重要基因表达和活动的机制 外周细胞膜蛋白对可获得性的反应 膜结合部位。

DESCRIPTION (provided by applicant) The PutA protein from Salmonella is a complex multifunctional protein that functions as a flavin dehydrogenase when associated with the membrane and as a transcriptional repressor when located in the cytoplasm. In addition, PutA is autophosphorylated on serine, threonine, and tyrosine residues in vivo and in vitro. PutA protein contains many serine, threonine, and tyrosine residues, and the positions of the serine, threonine, and tyrosine residues that are phosphorylated is unknown. Furthermore, although a model has been proposed that phosphorylation limits the toxic accumulation of excess PutA in the membrane, because it has been impossible to directly test this hypothesis, the function of PutA autophosphorylation is unknown. The primary goals of this research are to identify the sites within PutA that are phosphorylated, to construct mutations that alter phosphorylation of these sites, and to determine the effect of these mutations on each of the functions of PutA. In addition, this research will define the functional domains of PutA protein. These studies may reveal mechanisms used to coordinate the expression and activity of important peripheral membrane proteins in response to the availability of membrane-binding sites.