Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9

被引：652

作者：

Tatham, MH ^{[1
]}

Jaffray, E ^{[1
]}

Vaughan, OA ^{[1
]}

Desterro, JMP ^{[1
]}

Botting, CH ^{[1
]}

Naismith, JH ^{[1
]}

Hay, RT ^{[1
]}

机构：

[1] Univ St Andrews, Inst Biomol Sci, St Andrews KY16 5ST, Fife, Scotland

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2001年 / 276卷 / 38期

关键词：

D O I：

10.1074/jbc.M104214200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Conjugation of the small ubiquitin-like modifier SUMO-1/SMT3C/Sentrin-1 to proteins in vitro is dependent on a heterodimeric El (SAE1/SAE2) and an E2 (Ubc9). Although SUMO-2/SMT3A/Sentrin-3 and SUMO-3/SMT3B/Sentrin-2 share 50% sequence identity with SUMO-1, they are functionally distinct. Inspection of the SUMO-2 and SUMO-3 sequences indicates that they both contain the sequence psi KXE, which represents the consensus SUMO modification site. As a consequence SAE1/SAE2 and Ubc9 catalyze the formation of polymeric chains of SUMO-2 and SUMO-3 on protein substrates in vitro, and SUMO-2 chains are detected in vivo. The ability to form polymeric chains is not shared by SUMO-1 and although all SUMO species use the same conjugation machinery, modification by SUMO-1 and SUMO-2/-3 may have distinct functional consequences.

引用

页码：35368 / 35374

页数：7

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