Toolbox for chemically synthesized histone proteins

Koki Nakatsu; Gosuke Hayashi; Akimitsu Okamoto

doi:10.1016/j.cbpa.2020.04.016

Toolbox for chemically synthesized histone proteins

Curr Opin Chem Biol. 2020 Oct:58:10-19. doi: 10.1016/j.cbpa.2020.04.016. Epub 2020 May 27.

Authors

Koki Nakatsu¹, Gosuke Hayashi², Akimitsu Okamoto³

Affiliations

¹ Department of Chemistry and Biotechnology, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
² Department of Biomolecular Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan. Electronic address: hayashi@chembio.nagoya-u.ac.jp.
³ Department of Chemistry and Biotechnology, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan; Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo 153-8904, Japan. Electronic address: okamoto@chembio.t.u-tokyo.ac.jp.

PMID: 32473259
DOI: 10.1016/j.cbpa.2020.04.016

Abstract

Histone post-translational modifications play significant roles in gene regulation processes. Among many approaches, chemical protein synthesis has been a successful and promising method for the preparation of homogeneous products of site-specifically modified histones for elucidation of their biological significance. In this short review, we describe the recent advances in synthetic toolbox for histone proteins such as thioester precursors, chemical ubiquitination, and one-pot peptide ligation.

Keywords: Chemical protein synthesis; Histone; Native chemical ligation; Post-translational modifications.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Chemistry Techniques, Synthetic
Esters / chemistry
Histones / chemical synthesis*
Histones / metabolism*
Peptides / chemistry
Ubiquitination

Substances

Esters
Histones
Peptides