Hesterkamp T, Bukau B
Zentrum für Molekulare Biologie, Universität Heidelberg, Germany.
FEBS Lett. 1996 Jun 24;389(1):32-4. doi: 10.1016/0014-5793(96)00582-0.
E. coli trigger factor is an abundant cytosolic protein originally identified by its ability to maintain the precursor of a secretory protein in a translocation competent form. Recent studies shed new light on the function of this protein. Trigger factor was found to be a peptidyl-prolyl-cisltrans-isomerase capable of catalysing protein folding in vitro, to associate with nascent cytosolic and secretory polypeptide chains, and to cooperate with the GroEL chaperone in promoting proteolysis of an unstable polypeptide in vivo. These findings suggest roles for trigger factor in various folding processes of secretory as well as cytosolic proteins.
大肠杆菌触发因子是一种丰富的胞质蛋白，最初是因其能将分泌蛋白前体维持在易位活性形式而被鉴定出来的。最近的研究为该蛋白的功能提供了新的线索。触发因子被发现是一种肽基脯氨酰顺反异构酶，能够在体外催化蛋白质折叠，与新生的胞质和分泌多肽链结合，并在体内与GroEL伴侣蛋白协同促进不稳定多肽的蛋白水解。这些发现表明触发因子在分泌蛋白和胞质蛋白的各种折叠过程中发挥作用。
