Synlett 2017; 28(15): 1907-1912
DOI: 10.1055/s-0036-1590794
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© Georg Thieme Verlag Stuttgart · New York

Convergent Total Synthesis of Histone H2B Protein with Site-Specific Ubiquitination at Lys120

Yun-Kun Qi, Qiao-Qiao He, Hua-Song Ai, Jia-Bin Li*, Ji-Shen Zheng*
This work was funded by the National Natural Science Foundation of China (grant number 21402206), the Natural Science Foundation of Anhui Province (1508085QB30) and the Beijing National Laboratory for Molecular Sciences (No. 20140124).
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Publication History

Received: 13 April 2017

Accepted after revision: 28 May 2017

Publication Date:
11 July 2017 (eFirst)

Published as part of the Cluster Recent Advances in Protein and Peptide Synthesis

Abstract

Histone H2B Lys120 mono-ubiquitylation (H2BK120Ub) plays an important role in regulating gene expression and diverse nuclear processes. For biochemical and biophysical studies of this dynamic post-translational modification, access to homogeneous and workable amount of H2BK120Ub is obligatory. Here we report a new strategy for the convergent total chemical synthesis of homogenous histone H2BK120Ub on multi-milligram scale through the combination of hydrazide-based native chemical ligation and acid-cleavable auxiliary-mediated ligation of peptide hydrazides. The synthetic H2BK120Ub could be efficiently incorporated into nucleosomes, which may provide valuable materials for the biochemical and structural studies of nucleosome complexes involving H2BK120Ub.

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