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Sirtuin‐Derived Covalent Binder for the Selective Recognition of Protein Crotonylation.
- Source :
-
Angewandte Chemie . Aug2022, Vol. 134 Issue 31, p1-6. 6p. - Publication Year :
- 2022
-
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. [ABSTRACT FROM AUTHOR]
- Subjects :
- *POST-translational modification
*SIRTUINS
*PROTEINS
*AMINO acids
Subjects
Details
- Language :
- English
- ISSN :
- 00448249
- Volume :
- 134
- Issue :
- 31
- Database :
- Academic Search Index
- Journal :
- Angewandte Chemie
- Publication Type :
- Academic Journal
- Accession number :
- 158166060
- Full Text :
- https://doi.org/10.1002/ange.202205522