Darwin K Heran
Department of Microbiology, New York University School of Medicine, 550 First Avenue MSB 236, New York, New York 10016, USA.
Nat Rev Microbiol. 2009 Jul;7(7):485-91. doi: 10.1038/nrmicro2148. Epub 2009 Jun 1.
Proteasomes are ATP-dependent, multisubunit proteases that are found in all eukaryotes and archaea and some bacteria. In eukaryotes, the small protein ubiquitin is covalently attached in a post-translational manner to proteins that are targeted for proteasomal degradation. Despite the presence of proteasomes in many prokaryotes, ubiquitin or other post-translational protein modifiers were presumed to be absent from these organisms. Recently a prokaryotic ubiquitin-like protein, Pup, was found to target proteins for proteolysis by the Mycobacterium tuberculosis proteasome. The discovery of this ubiquitin-like modifier opens up the possibility that other bacteria may also have small post-translational protein tagging systems, with the ability to affect cellular processes.
蛋白酶体是一种依赖ATP的多亚基蛋白酶,存在于所有真核生物、古细菌以及一些细菌中。在真核生物中,小蛋白泛素以翻译后修饰的方式共价连接到靶向蛋白酶体降解的蛋白质上。尽管许多原核生物中存在蛋白酶体,但这些生物体中普遍认为不存在泛素或其他翻译后蛋白质修饰因子。最近,一种原核生物泛素样蛋白Pup被发现可将蛋白质靶向结核分枝杆菌蛋白酶体进行蛋白水解。这种泛素样修饰因子的发现开启了一种可能性,即其他细菌可能也具有小型翻译后蛋白质标记系统,能够影响细胞过程。