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Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants
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 th...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3796536/ https://www.ncbi.nlm.nih.gov/pubmed/24155879 http://dx.doi.org/10.1371/journal.pone.0075985 |
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author | Yuan, Xiaowei Zhang, Shizhong Sun, Meihong Liu, Shiyang Qi, Baoxiu Li, Xinzheng |
author_facet | Yuan, Xiaowei Zhang, Shizhong Sun, Meihong Liu, Shiyang Qi, Baoxiu Li, Xinzheng |
author_sort | Yuan, Xiaowei |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3796536 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-37965362013-10-23 Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants Yuan, Xiaowei Zhang, Shizhong Sun, Meihong Liu, Shiyang Qi, Baoxiu Li, Xinzheng PLoS One Research Article 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. Public Library of Science 2013-10-14 /pmc/articles/PMC3796536/ /pubmed/24155879 http://dx.doi.org/10.1371/journal.pone.0075985 Text en © 2013 Yuan et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Yuan, Xiaowei Zhang, Shizhong Sun, Meihong Liu, Shiyang Qi, Baoxiu Li, Xinzheng Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants |
title | Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants |
title_full | Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants |
title_fullStr | Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants |
title_full_unstemmed | Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants |
title_short | Putative DHHC-Cysteine-Rich Domain S-Acyltransferase in Plants |
title_sort | putative dhhc-cysteine-rich domain s-acyltransferase in plants |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3796536/ https://www.ncbi.nlm.nih.gov/pubmed/24155879 http://dx.doi.org/10.1371/journal.pone.0075985 |
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