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Study on the Cellular Regulation and Function of Lysine Malonylation, Glutarylation and Crotonylation pp 97–121Cite as

Identification of Sirt3 as an ‘Eraser’ for Histone Lysine Crotonylation Marks Using a Chemical Proteomics Approach

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Abstract

Increasing evidences have indicated histone posttranslational modifications (PTMs) play crucial roles in regulating a wide range of chromatin-templated nuclear processes, such as gene transcription, DNA replication and DNA damage repair [1]. PTMs on histones have been proposed to serve as histone code that provides epigenetic information from a mother cell to daughter cells [2]. Histone code is under control of opposing enzymes that ‘write’ or ‘erase’ modifications on histones [1, 3]. Meanwhile, this epigenetic code could be translated by ‘reader’ proteins, which can recognize specific histone modifications, into biological readout, without alteration of genetic information [4, 5].

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Authors and Affiliations

  1. Department of Chemistry, The University of Hong Kong, Hong Kong, China

    Xiucong Bao

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Correspondence to Xiucong Bao .

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Bao, X. (2020). Identification of Sirt3 as an ‘Eraser’ for Histone Lysine Crotonylation Marks Using a Chemical Proteomics Approach. In: Study on the Cellular Regulation and Function of Lysine Malonylation, Glutarylation and Crotonylation. Springer Theses. Springer, Singapore. https://doi.org/10.1007/978-981-15-2509-4_5

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