Issue 28, 2021

Diverse protein manipulations with genetically encoded glutamic acid benzyl ester

Abstract

Site-specific modification of proteins has significantly advanced the use of proteins in biological research and therapeutics development. Among various strategies aimed at this end, genetic code expansion (GCE) allows structurally and functionally distinct non-canonical amino acids (ncAAs) to be incorporated into specific sites of a protein. Herein, we genetically encode an esterified glutamic acid analogue (BnE) into proteins, and demonstrate that BnE can be applied in different types of site-specific protein modifications, including N-terminal pyroglutamation, caging Glu in the active site of a toxic protein, and endowing proteins with metal chelator hydroxamic acid and versatile reactive handle acyl hydrazide. Importantly, novel epigenetic mark Gln methylation is generated on histones via the derived acyl hydrazide handle. This work provides useful and unique tools to modify proteins at specific Glu or Gln residues, and complements the toolbox of GCE.

Graphical abstract: Diverse protein manipulations with genetically encoded glutamic acid benzyl ester

Supplementary files

Article information

Article type
Edge Article
Submitted
05 Apr. 2021
Accepted
16 Jūn. 2021
First published
17 Jūn. 2021
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2021,12, 9778-9785

Diverse protein manipulations with genetically encoded glutamic acid benzyl ester

X. Yang, H. Miao, R. Xiao, L. Wang, Y. Zhao, Q. Wu, Y. Ji, J. Du, H. Qin and W. Xuan, Chem. Sci., 2021, 12, 9778 DOI: 10.1039/D1SC01882E

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