Activity-based diubiquitin probes for elucidating the linkage specificity of deubiquitinating enzymes

Guorui Li; Qin Liang; Ping Gong; Adam H Tencer; Zhihao Zhuang

doi:10.1039/c3cc47382a

Activity-based diubiquitin probes for elucidating the linkage specificity of deubiquitinating enzymes

Chem Commun (Camb). 2014 Jan 7;50(2):216-8. doi: 10.1039/c3cc47382a.

Authors

Guorui Li¹, Qin Liang, Ping Gong, Adam H Tencer, Zhihao Zhuang

Affiliation

¹ Department of Chemistry and Biochemistry, University of Delaware, 214A Drake Hall, Newark, DE 19716, USA. zzhuang@udel.edu.

Abstract

We report a new class of deubiquitinating enzyme (DUB) probes that resemble the native diubiquitin with a same linkage size and contain a Michael addition acceptor for trapping the DUB active-site cysteine. Both K63- and K48-linked diubiquitin probes were generated using a facile chemical ligation method. The diUb probes were demonstrated to label DUBs from different families and revealed intrinsic linkage specificities of DUBs.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Animals
Catalytic Domain
Electrophoresis, Polyacrylamide Gel
Humans
Models, Molecular
Molecular Probe Techniques
Molecular Probes / chemistry*
Ubiquitin-Specific Proteases / chemistry*

Substances

Molecular Probes
Ubiquitin-Specific Proteases

Abstract

Publication types

MeSH terms

Substances

Grants and funding