Post-Transitional Modification: Salmonella PutA Protein

描述（由申请人提供） 来自沙门氏菌的PutA蛋白是一种复杂的多功能蛋白， 当与膜结合时作为黄素脱氢酶起作用， 当位于细胞质中时，转录阻遏物。此外，PutA是 丝氨酸、苏氨酸和酪氨酸残基上的自磷酸化， 体外PutA蛋白含有许多丝氨酸、苏氨酸和酪氨酸残基， 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， 磷酸化限制了过量PutA在膜中的毒性积累， 因为不可能直接检验这个假设， PutA自身磷酸化的机制尚不清楚。本研究的主要目标是 为了鉴定PutA中磷酸化的位点， 突变改变这些位点的磷酸化，并确定 这些突变对PutA的每种功能的影响。另外这款 研究将确定PutA蛋白的功能结构域。这些研究可能 揭示了用于协调重要的表达和活动的机制， 外周膜蛋白的可用性， 膜结合位点。

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.