Kim Keun Il, Baek Sung Hee, Chung Chin Ha
NRL of Protein Biochemistry, School of Biological Sciences, Seoul National University, Seoul, Korea.
J Cell Physiol. 2002 Jun;191(3):257-68. doi: 10.1002/jcp.10100.
Small ubiquitin-related modifier (SUMO) is a member of a ubiquitin-like protein family that regulates cellular function of a variety of target proteins. SUMO and ubiquitin are synthesized as precursors that need to be processed prior to conjugation to target proteins, and their mature forms have a similar tertiary structure. The mechanism for SUMO conjugation is also analogous to that of the ubiquitin system, such as the utilization of E1, E2, and E3 cascade enzymes. However, the biological consequence of SUMO modification is quite different from that of the ubiquitin system. Whereas ubiquitination of most proteins is for the degradative pathway, SUMO modification of target proteins is involved in nuclear protein targeting, formation of subnuclear structures, regulation of transcriptional activities or DNA binding abilities of transcription factors, and control of protein stability. This review will summarize the recent progress made in the enzymology of SUMO and its biological significance.
小泛素相关修饰物(SUMO)是泛素样蛋白家族的成员,可调节多种靶蛋白的细胞功能。SUMO和泛素以前体形式合成,在与靶蛋白结合之前需要进行加工,并且它们的成熟形式具有相似的三级结构。SUMO结合的机制也类似于泛素系统,例如利用E1、E2和E3级联酶。然而,SUMO修饰的生物学后果与泛素系统有很大不同。大多数蛋白质的泛素化是用于降解途径,而靶蛋白的SUMO修饰则参与核蛋白靶向、亚核结构的形成、转录活性的调节或转录因子的DNA结合能力以及蛋白质稳定性的控制。本综述将总结SUMO酶学及其生物学意义方面的最新进展。