Molière Noël, Turgay Kürşad
Leibniz Universität Hannover, Institut für Mikrobiologie, Schneiderberg 50, D-30167, Hannover, Germany.
Mol Microbiol. 2014 Aug;93(4):583-6. doi: 10.1111/mmi.12696. Epub 2014 Jul 7.
Hsp100/Clp protease complexes are molecular machines important for cellular protein homeostasis and are concurrently embedded in the control of various signal transduction networks by regulatory proteolysis. In Mycobacteria, the genes encoding the components of these Hsp100/Clp protease complexes are essential for growth and were identified as targets for antibiotics, with a new antimicrobial mechanism, that are active on slow growing or even dormant cells. Schmitz and Sauer (2014) report the biochemical characterization of mycobacterial Hsp100/Clp protease complexes actively degrading folded substrate proteins. Their results suggest an unusual activation mechanism for this protease complex and will set the stage for further mechanistic studies of antibiotics acting on this new cellular target.
热休克蛋白100/Clp蛋白酶复合体是对细胞蛋白质稳态很重要的分子机器，同时通过调节性蛋白水解作用参与各种信号转导网络的调控。在分枝杆菌中，编码这些热休克蛋白100/Clp蛋白酶复合体组分的基因对生长至关重要，并被确定为具有新抗菌机制的抗生素作用靶点，这些抗生素对生长缓慢甚至休眠的细胞具有活性。施密茨和绍尔（2014年）报道了分枝杆菌热休克蛋白100/Clp蛋白酶复合体对折叠底物蛋白进行主动降解的生化特性。他们的结果表明该蛋白酶复合体存在一种不同寻常的激活机制，并将为作用于这一新细胞靶点的抗生素的进一步机制研究奠定基础。
