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Identification of SET Domain-Containing Proteins in Gossypium raimondii and Their Response to High Temperature Stress
SET (Su(var), E(z), and Trithorax) domain-containing proteins play an important role in plant development and stress responses through modifying lysine methylation status of histone. Gossypium raimondii may be the putative contributor of the D-subgenome of economical crops allotetraploid G. hirsutum...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5013442/ https://www.ncbi.nlm.nih.gov/pubmed/27601353 http://dx.doi.org/10.1038/srep32729 |
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author | Huang, Yong Mo, Yijia Chen, Pengyun Yuan, Xiaoling Meng, Funing Zhu, Shengwei Liu, Zhi |
author_facet | Huang, Yong Mo, Yijia Chen, Pengyun Yuan, Xiaoling Meng, Funing Zhu, Shengwei Liu, Zhi |
author_sort | Huang, Yong |
collection | PubMed |
description | SET (Su(var), E(z), and Trithorax) domain-containing proteins play an important role in plant development and stress responses through modifying lysine methylation status of histone. Gossypium raimondii may be the putative contributor of the D-subgenome of economical crops allotetraploid G. hirsutum and G. barbadense and therefore can potentially provide resistance genes. In this study, we identified 52 SET domain-containing genes from G. raimondii genome. Based on conserved sequences, these genes are grouped into seven classes and are predicted to catalyze the methylation of different substrates: GrKMT1 for H3K9me, GrKMT2 and GrKMT7 for H3K4me, GrKMT3 for H3K36me, GrKMT6 for H3K27me, but GrRBCMT and GrS-ET for nonhistones substrate-specific methylation. Seven pairs of GrKMT and GrRBCMT homologous genes are found to be duplicated, possibly one originating from tandem duplication and five from a large scale or whole genome duplication event. The gene structure, domain organization and expression patterns analyses suggest that these genes’ functions are diversified. A few of GrKMTs and GrRBCMTs, especially for GrKMT1A;1a, GrKMT3;3 and GrKMT6B;1 were affected by high temperature (HT) stress, demonstrating dramatically changed expression patterns. The characterization of SET domain-containing genes in G. raimondii provides useful clues for further revealing epigenetic regulation under HT and function diversification during evolution. |
format | Online Article Text |
id | pubmed-5013442 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-50134422016-09-12 Identification of SET Domain-Containing Proteins in Gossypium raimondii and Their Response to High Temperature Stress Huang, Yong Mo, Yijia Chen, Pengyun Yuan, Xiaoling Meng, Funing Zhu, Shengwei Liu, Zhi Sci Rep Article SET (Su(var), E(z), and Trithorax) domain-containing proteins play an important role in plant development and stress responses through modifying lysine methylation status of histone. Gossypium raimondii may be the putative contributor of the D-subgenome of economical crops allotetraploid G. hirsutum and G. barbadense and therefore can potentially provide resistance genes. In this study, we identified 52 SET domain-containing genes from G. raimondii genome. Based on conserved sequences, these genes are grouped into seven classes and are predicted to catalyze the methylation of different substrates: GrKMT1 for H3K9me, GrKMT2 and GrKMT7 for H3K4me, GrKMT3 for H3K36me, GrKMT6 for H3K27me, but GrRBCMT and GrS-ET for nonhistones substrate-specific methylation. Seven pairs of GrKMT and GrRBCMT homologous genes are found to be duplicated, possibly one originating from tandem duplication and five from a large scale or whole genome duplication event. The gene structure, domain organization and expression patterns analyses suggest that these genes’ functions are diversified. A few of GrKMTs and GrRBCMTs, especially for GrKMT1A;1a, GrKMT3;3 and GrKMT6B;1 were affected by high temperature (HT) stress, demonstrating dramatically changed expression patterns. The characterization of SET domain-containing genes in G. raimondii provides useful clues for further revealing epigenetic regulation under HT and function diversification during evolution. Nature Publishing Group 2016-09-07 /pmc/articles/PMC5013442/ /pubmed/27601353 http://dx.doi.org/10.1038/srep32729 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Huang, Yong Mo, Yijia Chen, Pengyun Yuan, Xiaoling Meng, Funing Zhu, Shengwei Liu, Zhi Identification of SET Domain-Containing Proteins in Gossypium raimondii and Their Response to High Temperature Stress |
title | Identification of SET Domain-Containing Proteins in Gossypium raimondii and Their Response to High Temperature Stress |
title_full | Identification of SET Domain-Containing Proteins in Gossypium raimondii and Their Response to High Temperature Stress |
title_fullStr | Identification of SET Domain-Containing Proteins in Gossypium raimondii and Their Response to High Temperature Stress |
title_full_unstemmed | Identification of SET Domain-Containing Proteins in Gossypium raimondii and Their Response to High Temperature Stress |
title_short | Identification of SET Domain-Containing Proteins in Gossypium raimondii and Their Response to High Temperature Stress |
title_sort | identification of set domain-containing proteins in gossypium raimondii and their response to high temperature stress |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5013442/ https://www.ncbi.nlm.nih.gov/pubmed/27601353 http://dx.doi.org/10.1038/srep32729 |
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