Abstract
Reversible protein acetylation catalyzed by histone acetyltransferases (HATs) and histone deacetylases (HDACs) is an essential post-translational modification (PTM) mechanism which correlates largely with epigenetic gene regulation such as transcriptional activation, DNA replication, histone deposition, and DNA repair. Dysfunction of histone acetylation and the aberrant activity of HATs/HDACs is often associated with the pathogenesis of numerous diseases, especially cancer. Therefore, developing potent and specific analytical methods for HATs/HDACs is important for fundamental biochemical research, disease diagnosis and treatment, and drug development. This paper briefly summarizes the general design strategies used in HAT/HDAC sensors, gives a systematic overview of recent advances in the analytical methods for HAT/HDAC enzymatic analysis, classifies these methods by their biorecognition mechanisms and relative applications either in vitro or in living cells, then outlines challenges faced by these bioanalytical methods and offers perspectives on future developments.
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Acknowledgments
This work was financially supported by the National Natural Science Foundation of China (Nos. 21222507, 21175036, 21235002, and 21475038), the National Basic Research Program of China (973 Program, No. 2011CB911002), the Foundation for Innovative Research Groups of NSFC (Grant 21221003), and the Natural Science Foundation of Hunan Province (No. 2015JJ1005).
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Published in the topical collection featuring Young Investigators in Analytical and Bioanalytical Science with guest editors S. Daunert, A. Baeumner, S. Deo, J. Ruiz Encinar, and L. Zhang.
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Li, P., Han, Y., Li, Y. et al. Bioanalytical approaches for the detection of protein acetylation-related enzymes. Anal Bioanal Chem 408, 2659–2668 (2016). https://doi.org/10.1007/s00216-016-9304-7
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DOI: https://doi.org/10.1007/s00216-016-9304-7