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Updated: May 6, 2026

Detection of Histone Modifications in Plant Leaves
Published on: September 23, 2011
Putative DHHC-cysteine-rich domain S-acyltransferase in plants
Xiaowei Yuan1, Shizhong Zhang, Meihong Sun
1State Key Laboratory of Crop Biology, Shandong Agricultural University, Tai-An, Shandong 271018, China ; Huasheng Agriculture Limited Liability Company, Qingzhou, Shandong 262500, China ; Qingzhou City Bureau of Agriculture, Qingzhou, Shandong 262500, China.
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.
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