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Published on: April 10, 2020
Sirtuin-Derived Covalent Binder for the Selective Recognition of Protein Crotonylation
Yanli Ji1, Lin Sun1, Yao Chen2
1State Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University, Tianjin, 300071, China.
Abstract:
Lysine crotonylation (Kcr) is increasingly recognized as a key protein post-translational modification. However, selective detection and enrichment of crotonylated proteins remains a challenging task. Herein we present a covalent binder for the selective recognition of protein crotonylation. Based on proximity-induced crosslinking, a bacterial sirtuin (CobB) was remodeled with genetically installed thiol-bearing noncanonical amino acids at the Kcr-interacting site, which subsequently could react with Kcr sites in a unique NAD+ -dependent manner. The covalent binder has been used to selectively recognize crotonylated proteins in extracted histone samples and in fixed cells.
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