Yu Angela Yeou Hsiung, Houry Walid A
Department of Biochemistry, University of Toronto, Medical Sciences Building, 1 King's College Circle, Toronto, ON, Canada M5S 1A8.
FEBS Lett. 2007 Jul 31;581(19):3749-57. doi: 10.1016/j.febslet.2007.04.076. Epub 2007 May 8.
Processes maintaining protein homeostasis in the cell are governed by the activities of molecular chaperones that mainly assist in the folding of polypeptide chains and by a large class of proteases that regulate protein levels through degradation. ClpP proteases define a distinctive family of cylindrical, energy-dependent serine proteases that are highly conserved throughout bacteria and eukaryota. They typically interact with ATP-dependent AAA+ chaperones that bind and unfold target substrates and then translocate them into ClpP for degradation. Structural and functional studies have provided a detailed view of the mechanism of function of this class of proteases.
细胞中维持蛋白质稳态的过程由分子伴侣的活性所调控，分子伴侣主要协助多肽链折叠，同时也由一大类通过降解来调节蛋白质水平的蛋白酶所调控。ClpP蛋白酶是一类独特的圆柱形、能量依赖型丝氨酸蛋白酶家族，在细菌和真核生物中高度保守。它们通常与依赖ATP的AAA+分子伴侣相互作用，这些分子伴侣结合并展开靶底物，然后将其转运到ClpP中进行降解。结构和功能研究为这类蛋白酶的功能机制提供了详细的见解。
