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Chemical Biology Approaches for Investigating the Functions of Lysine Acetyltransferases
Author(s) -
He Maomao,
Han Zhen,
Liu Liang,
Zheng Y. George
Publication year - 2018
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201704745
Subject(s) - acetylation , histone acetyltransferases , lysine , histone , acetyltransferases , epigenetics , computational biology , chemical biology , biology , biochemistry , function (biology) , sumo protein , ubiquitin , microbiology and biotechnology , dna , amino acid , gene
The side‐chain acetylation of lysine residues in histones and non‐histone proteins catalyzed by lysine acetyltransferases (KATs) represents a widespread posttranslational modification (PTM) in the eukaryotic cells. Lysine acetylation plays regulatory roles in major cellular pathways inside and outside the nucleus. In particular, KAT‐mediated histone acetylation has an effect on all DNA‐templated epigenetic processes. Aberrant expression and activation of KATs are commonly observed in human diseases, especially cancer. In recent years, the study of KAT functions in biology and disease has greatly benefited from chemical biology tools and strategies. In this Review, we present the past and current accomplishments in the design of chemical biology approaches for the interrogation of KAT activity and function. These methods and probes are classified according to their mechanisms of action and respective applications, with both strengths and limitations discussed.