期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 61, 期 31, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202205522
关键词
Enzymes; Noncanonical Amino Acid; Post-Translational Protein Modification; Protein Engineering; Sirtuin; Lysine Crotonylation
资金
- National Natural Science Foundation of China [21807061, 92156025]
- Natural Science Foundation of Tianjin [18JCYBJC41600]
- Youth Innovation Promotion Association of CAS [2018212]
This article introduces a covalent binder for the selective recognition of protein crotonylation. By proximity-induced crosslinking, CobB, a bacterial sirtuin, was modified to react selectively with crotonylated sites. The covalent binder has been successfully used to recognize crotonylated proteins in histone samples and fixed cells.
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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