NDLI: Protein ubiquitination and formation of polyubiquitin chains without ATP, E1 and E2 enzymes

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Back cover

Chemical Science Vol - 6 Issue - 2

Chemical Science Vol -5

Chemical Science Vol -4

Chemical Science Vol -3

Chemical Science Vol -2

Chemical Science Vol -1

Protein ubiquitination and formation of polyubiquitin chains without ATP, E1 and E2 enzymes

Content Provider	Royal Society of Chemistry (RSC)
Author	Statsyuk, Alexander V. Park, Sungjin Krist, David T.
Copyright Year	2015
Abstract	Studying protein ubiquitination is difficult due to the complexity of the E1–E2–E3 ubiquitination cascade. Here we report the discovery that C-terminal ubiquitin thioesters can undergo direct transthiolation with the catalytic cysteine of the model HECT E3 ubiquitin ligase Rsp5 to form a catalytically active Rsp5∼ubiquitin thioester (Rsp5∼Ub). The resulting Rsp5∼Ub undergoes efficient autoubiquitination, ubiquitinates protein substrates, and synthesizes polyubiquitin chains with native Ub isopeptide linkage specificity. Since the developed chemical system bypasses the need for ATP, E1 and E2 enzymes while maintaining the native HECT E3 mechanism, we named it “Bypassing System” (ByS). Importantly, ByS provides direct evidence that E2 enzymes are dispensable for K63 specific isopeptide bond formation between ubiquitin molecules by Rsp5 in vitro. Additionally, six other E3 enzymes including Nedd4-1, Nedd4-2, Itch, and Wwp1 HECT ligases, along with Parkin and HHARI RBR ligases processed Ub thioesters under ByS reaction conditions. These findings provide general mechanistic insights on protein ubiquitination, and offer new strategies for assay development to discover pharmacological modulators of E3 enzymes.
Starting Page	1770
Ending Page	1779
Page Count	10
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	6
Issue Number	3
Journal	Chemical Science
DOI	10.1039/c4sc02340d
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Ubiquitin Electronic Entertainment Expo Cysteine Ubiquitin ligase Thioester Isopeptide bond ATP Ub Protein C-terminus Adenosine triphosphate Parkin
Content Type	Text
Resource Type	Article
Subject	Chemistry

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Protein ubiquitination and formation of polyubiquitin chains without ATP, E1 and E2 enzymes

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Protein ubiquitination and formation of polyubiquitin chains without ATP, E1 and E2 enzymes