Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants

Xiaowei Yuan,Shizhong Zhang,Baoxiu Qi,Shiyang Liu,Xinzheng Li,Meihong Sun,Meng-Xiang Sun

doi:10.1371/journal.pone.0075985

Xiaowei Yuan, Shizhong Zhang + Show 5 more

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https://doi.org/10.1371/journal.pone.0075985

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Abstract

Protein S-acyltransferases (PATs) containing Asp-His-His-Cys within a Cys-rich domain (DHHC-CRD) are polytopic transmembrane proteins that are found in eukaryotic cells and mediate the S-acylation of target proteins. S-acylation is an important secondary and reversible modification that regulates the membrane association, trafficking and function of target proteins. However, little is known about the characteristics of PATs in plants. Here, we identified 804 PATs from 31 species with complete genomes. The analysis of the phylogenetic relationships suggested that all of the PATs fell into 8 groups. In addition, we analysed the phylogeny, genomic organization, chromosome localisation and expression pattern of PATs in Arabidopsis, Oryza sative, Zea mays and Glycine max. The microarray data revealed that PATs genes were expressed in different tissues and during different life stages. The preferential expression of the ZmPATs in specific tissues and the response of Zea mays to treatments with phytohormones and abiotic stress demonstrated that the PATs play roles in plant growth and development as well as in stress responses. Our data provide a useful reference for the identification and functional analysis of the members of this protein family.

Highlights

S-acylation refers to the reversible post-translational attachment of an acyl group to a cysteine residue via a thioester linkage [1,2]
A total of 804 proteins were identified as potential members of the DHHC-CRD-containing Protein S-acyltransferases (PATs) family within the 31 plant genomes that have been completely sequenced (Phytozome database: http://www.phytozome.net/)
We observed that all 31 species contained PAT proteins and the number of PATs ranged from 6 (Volvox carteri) to 52 (Panicum virgatum) (Fig. 1)

Summary

Introduction

S-acylation refers to the reversible post-translational attachment of an acyl group to a cysteine residue via a thioester linkage [1,2]. The most common fatty acid attached to cysteines is palmitate, and S-acylation is often called S-palmitoylation. Other acyl groups with different chain lengths and degrees of unsaturation can be added to cysteines in a similar manner [3,4]. S-acylation is one of a group of lipid modifications that occur on eukaryotic proteins [1]. S-acyl modification mainly affects membrane attachment and trafficking of proteins [5,6]. S-acyl modification is required for the dynamic association of proteins with membrane subdomains and for the cycling between different cellular membranes [7,8,9]. S-acylation can influence the stability of proteins, modulate the functions of proteins and mediate interactions between different proteins [9,10]

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