Perego M, Brannigan J A
Division of Cellular Biology, Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Peptides. 2001 Oct;22(10):1541-7. doi: 10.1016/s0196-9781(01)00490-9.
Aspartyl-phosphate phosphatases are integral components of the phosphorelay signal transduction system for sporulation initiation in Bacillus subtilis. The Rap and Spo0E families of protein phosphatases specifically dephosphorylate the sporulation response regulators Spo0F and Spo0A, respectively. The phosphatases interpret regulatory signals antithetical to sporulation and the Rap phosphatases are subject to inactivation by specific pentapeptides generated from an inactive peptide precursor. Additional regulatory signals are brought about by the complex activation circuit that generates the Phr pentapeptide inhibitors of Rap phosphatases. Phr peptide's recognition of the Rap phosphatase targets is remarkably specific. Specificity is dictated by the amino acid sequence of the pentapeptide. The identification of tetratricopeptide repeats in the Rap proteins may explain the mechanism by which Phr peptides bind to and inhibit the activity of Rap phosphatases.
天冬氨酰 - 磷酸磷酸酶是枯草芽孢杆菌中孢子形成起始的磷信号转导系统的组成部分。Rap和Spo0E家族的蛋白磷酸酶分别特异性地使孢子形成反应调节因子Spo0F和Spo0A去磷酸化。这些磷酸酶解读与孢子形成相反的调节信号，并且Rap磷酸酶会被由无活性肽前体产生的特定五肽失活。由产生Rap磷酸酶的Phr五肽抑制剂的复杂激活回路带来了额外的调节信号。Phr肽对Rap磷酸酶靶点的识别非常特异。特异性由五肽的氨基酸序列决定。Rap蛋白中四肽重复序列的鉴定可能解释了Phr肽结合并抑制Rap磷酸酶活性的机制。
