Molle Virginie, Girard-Blanc Christine, Kremer Laurent, Doublet Patricia, Cozzone Alain J, Prost Jean-François
Institut de Biologie et Chimie des Protéines, Université de Lyon, Centre National de la Recherche Scientifique, Lyon, France.
Biochem Biophys Res Commun. 2003 Sep 5;308(4):820-5. doi: 10.1016/s0006-291x(03)01476-1.
Protein PknE from Mycobacterium tuberculosis has been overproduced and purified, and its biochemical properties have been analyzed. This protein is shown to be a eukaryotic-like (Hanks'-type) protein kinase with a structural organization similar to that of membrane-bound eukaryotic sensor serine/threonine kinases. It consists of a N-terminal catalytic domain located in the cytoplasm, linked via a single transmembrane-spanning region to an extracellular C-terminal domain. The full-length enzyme, as well as the cytosolic domain alone, can autophosphorylate on serine and threonine residues. Such autokinase activity requires the presence of a lysine residue at position 45 in subdomain II, which is known to be essential also for eukaryotic kinase activity. Involvement of PknE in the transduction of external signals into the cytosol of bacteria is proposed.
结核分枝杆菌的蛋白PknE已被过量表达并纯化,其生化特性也已得到分析。该蛋白被证明是一种类真核(汉克斯型)蛋白激酶,其结构组织类似于膜结合的真核传感器丝氨酸/苏氨酸激酶。它由位于细胞质中的N端催化结构域组成,通过单个跨膜区域与细胞外C端结构域相连。全长酶以及单独的胞质结构域都可以在丝氨酸和苏氨酸残基上进行自磷酸化。这种自激酶活性需要亚结构域II中第45位赖氨酸残基的存在,已知该残基对真核激酶活性也至关重要。有人提出PknE参与将外部信号转导到细菌细胞质中。