Department of Chemistry, The Scripps Research Institute, Scripps Florida, Jupiter, Florida 33458, USA.
J Biol Chem. 2010 Jan 22;285(4):2221-6. doi: 10.1074/jbc.R109.077883. Epub 2009 Dec 2.
The ubiquitin-proteasome pathway (UPP) is responsible for most programmed turnover of proteins in eukaryotic cells, and this activity has been known for some time to be involved in transcriptional regulation. More recently, intersections of the UPP and transcription have been discovered that are not proteolytic in nature and appear to revolve around the chaperonin-like activities of the ATPases in the 19 S regulatory subunit of the proteasome. Moreover, monoubiquitylation, which does not signal degradation, has been found to be a key modification of many transcription factors and histones. These various non-proteolytic roles of the UPP in transcription are reviewed here, and plausible mechanistic models are discussed.
泛素-蛋白酶体途径（UPP）负责真核细胞中大多数蛋白质的程序性降解，这一活性在一段时间以来一直与转录调控有关。最近，人们发现 UPP 和转录之间存在一些非蛋白水解性质的交汇点，这些交汇点似乎围绕着蛋白酶体 19S 调节亚基中 ATP 酶的伴侣样活性。此外，单泛素化（monoubiquitylation），即不引发降解的泛素化，已被发现是许多转录因子和组蛋白的关键修饰。本文综述了 UPP 在转录中的这些各种非蛋白水解作用，并讨论了合理的机制模型。
