Protein Acetylation/Deacetylation: A Potential Strategy for Fungal Infection Control.

Junzhu Chen,Qiong Liu,Lingbing Zeng,Xiaotian Huang

doi:10.3389/fmicb.2020.574736

Abstract

Protein acetylation is a universal post-translational modification that fine-tunes the major cellular processes of many life forms. Although the mechanisms regulating protein acetylation have not been fully elucidated, this modification is finely tuned by both enzymatic and non-enzymatic mechanisms. Protein deacetylation is the reverse process of acetylation and is mediated by deacetylases. Together, protein acetylation and deacetylation constitute a reversible regulatory protein acetylation network. The recent application of mass spectrometry-based proteomics has led to accumulating evidence indicating that reversible protein acetylation may be related to fungal virulence because a substantial amount of virulence factors are acetylated. Additionally, the relationship between protein acetylation/deacetylation and fungal drug resistance has also been proven and the potential of deacetylase inhibitors as an anti-infective treatment has attracted attention. This review aimed to summarize the research progress in understanding fungal protein acetylation/deacetylation and discuss the mechanism of its mediation in fungal virulence, providing novel targets for the treatment of fungal infection.

Highlights

The post-translational modification (PTM) of proteins is a major regulatory mechanism in all life forms
As a common PTM, protein acetylation plays an essential role in metabolism, virulence, transcription, and translation, among other processes
Acetylation is primarily catalyzed by specific acetyltransferases but can occur due to the non-enzymatic reactions of acetyl phosphates

Summary

Introduction

The post-translational modification (PTM) of proteins is a major regulatory mechanism in all life forms. PTM refers to the chemical modification of amino acid residues in proteins by the addition of different chemical groups, which confer new properties on modified proteins, including changes in enzyme activity, subcellular localization, interaction partners, protein stability, and DNA binding (Mann and Jensen, 2003; Verdin and Ott, 2015). Nearly 200 different types of PTMs have been identified, including acetylation, phosphorylation, alkylation, methylation, ubiquitination, and glycosylation (Garavelli, 2004). Protein acetylation, which refers to the covalent binding of an acetyl group to an amino acid residue of a protein, is the most well-known PTM besides phosphorylation (Ali et al, 2018). The most widely studied protein acetylation is that of lysine residues, acetylation of serine and threonine side chains has been reported (Tang and Yu, 2019). Unless otherwise specified, in this review, acetylation refers only to that of lysine residues

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