Issue 7, 2011
From the journal:

Chemical Communications

Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups†

Carlos A. Castañeda,ab   Jia Liu,b   Tanuja R. Kashyap,ab   Rajesh K. Singh,ab   David Fushman*ab  and  T. Ashton Cropp*b  

* Corresponding authors

a Center for Biomolecular Structure and Organization, University of Maryland, College Park, Maryland, USA
E-mail: fushman@umd.edu
Fax: +1 301 314 0386

b Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland, USA
E-mail: acropp@gmail.com

Abstract

E2 enzymes catalyze the ATP-dependent polymerization of polyubiquitin chains which function as molecular signals in the regulation of numerous cellular processes. Here we present a method that uses genetically encoded unnatural amino acids to halt and re-start ubiquitin polymerization providing access to natural-linkage, precision-length ubiquitin chains that can be used for biochemical, structural, and dynamics studies.

Graphical abstract: Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups

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Article information

DOI
https://doi.org/10.1039/C0CC04868B
Article type
Communication
Submitted
09 Nov 2010
Accepted
10 Dec 2010
First published
06 Jan 2011

Chem. Commun., 2011,47, 2026-2028

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Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups

C. A. Castañeda, J. Liu, T. R. Kashyap, R. K. Singh, D. Fushman and T. A. Cropp, Chem. Commun., 2011, 47, 2026 DOI: 10.1039/C0CC04868B

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