Wawrzynow A, Banecki B, Zylicz M
Department of Molecular and Cellular Biology, University of Gdansk, Poland.
Mol Microbiol. 1996 Sep;21(5):895-9. doi: 10.1046/j.1365-2958.1996.421404.x.
The Clp ATPases were originally identified as a regulatory component of the bacterial ATP-dependent Clp serine proteases. Proteins homologous to the Escherichia coli Clp ATPases (ClpA, B, X or Y) have been identified in every organism examined so far. Recent data suggest that the Clp ATPases are not only specificity factors which help to 'present' various protein substrates to the ClpP or other catalytic proteases, but are also molecular chaperones which can function independently of ClpP. This review discusses the recent evidence that the Clp ATPases are indeed molecular chaperones capable of either repairing proteins damaged during stress conditions or activating the initiation proteins for Mu, lambda or P1 DNA replication. A mechanism is suggested to explain how the Clp ATPases 'decide' whether to repair or destroy their protein substrates.
Clp ATP酶最初被鉴定为细菌ATP依赖性Clp丝氨酸蛋白酶的一种调节成分。迄今为止，在每一种被检测的生物体中都发现了与大肠杆菌Clp ATP酶（ClpA、B、X或Y）同源的蛋白质。最近的数据表明，Clp ATP酶不仅是有助于将各种蛋白质底物“呈递”给ClpP或其他催化蛋白酶的特异性因子，而且还是能够独立于ClpP发挥作用的分子伴侣。本综述讨论了最近的证据，即Clp ATP酶确实是分子伴侣，能够修复应激条件下受损的蛋白质或激活Mu、λ或P1 DNA复制的起始蛋白。本文提出了一种机制来解释Clp ATP酶如何“决定”是修复还是降解其蛋白质底物。
