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

Yuan, X, Zhang, S, Sun, M, Liu, S, Qi, B and Li, X (2013) Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants. PLoS One, 8 (10). ISSN 1932-6203

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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.

Item Type: Article
Uncontrolled Keywords: Science & Technology; Multidisciplinary Sciences; Science & Technology - Other Topics; MULTIPLE SEQUENCE ALIGNMENT; PROTEIN PALMITOYLATION; TIP GROWTH; ACYLATION; GENE; LOCALIZATION; MEMBRANE; ACID; RAS; CALCIUM
Subjects: R Medicine > RM Therapeutics. Pharmacology
R Medicine > RV Botanic, Thomsonian, and eclectic medicine
Divisions: Pharmacy & Biomolecular Sciences
Publisher: Public Library of Science
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Date Deposited: 06 Mar 2020 11:27
Last Modified: 04 Sep 2021 07:46
DOI or ID number: 10.1371/journal.pone.0075985
URI: https://researchonline.ljmu.ac.uk/id/eprint/12418
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