E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer

被引：117

作者：

Eletr, ZM

Huang, DT

Duda, DM

Schulman, BA

Kuhlman, B ^{[1
]}

机构：

[1] Univ N Carolina, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA

[2] St Jude Childrens Res Hosp, Dept Biol Struct, Memphis, TN 38105 USA

[3] St Jude Childrens Res Hosp, Dept Genet & Tumor Cell Biol, Memphis, TN 38105 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2005年 / 12卷 / 10期

关键词：

D O I：

10.1038/nsmb984

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：

During ubiquitin ligation, an E2 conjugating enzyme receives ubiquitin from an E1 enzyme and then interacts with an E3 ligase to modify substrates. Competitive binding experiments with three human E2- E3 protein pairs show that the binding of E1s and of E3s to E2s are mutually exclusive. These results imply that polyubiquitination requires recycling of E2 for addition of successive ubiquitins to substrate.

引用

页码：933 / 934

页数：2

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