Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum)
Histone acetylation and deacetylation at the N-terminus of histone tails play crucial roles in the regulation of eukaryotic gene activity. Histone acetylation and deacetylation are catalyzed by histone acetyltransferases and histone deacetylases (HDACs), respectively. A growing number of studies hav...
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2015
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pubmed-42850132015-01-21 Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum) Zhao, Linmao Lu, Jingxia Zhang, Jianxia Wu, Pei-Ying Yang, Songguang Wu, Keqiang Plant Science Histone acetylation and deacetylation at the N-terminus of histone tails play crucial roles in the regulation of eukaryotic gene activity. Histone acetylation and deacetylation are catalyzed by histone acetyltransferases and histone deacetylases (HDACs), respectively. A growing number of studies have demonstrated the importance of histone deacetylation/acetylation on genome stability, transcriptional regulation, development and response to stress in Arabidopsis. However, the biological functions of HDACs in tomato have not been investigated previously. Fifteen HDACs identified from tomato (Solanum lycopersicum) can be grouped into RPD3/HDA1, SIR2 and HD2 families based on phylogenetic analysis. Meanwhile, 10 members of the RPD3/HDA1 family can be further subdivided into four groups, namely Class I, Class II, Class III, and Class IV. High similarities of protein sequences and conserved domains were identified among SlHDACs and their homologs in Arabidopsis. Most SlHDACs were expressed in all tissues examined with different transcript abundance. Transient expression in Arabidopsis protoplasts showed that SlHDA8, SlHDA1, SlHDA5, SlSRT1 and members of the HD2 family were localized to the nucleus, whereas SlHDA3 and SlHDA4 were localized in both the cytoplasm and nucleus. The difference in the expression patterns and subcellular localization of SlHDACs suggest that they may play distinct functions in tomato. Furthermore, we found that three members of the RPD3/HDA1 family, SlHDA1, SIHDA3 and SlHDA4, interacted with TAG1 (TOMATO AGAMOUS1) and TM29 (TOMATO MADS BOX29), two MADS-box proteins associated with tomato reproductive development, indicating that these HDACs may be involved in gene regulation in reproductive development. Frontiers Media S.A. 2015-01-06 /pmc/articles/PMC4285013/ /pubmed/25610445 http://dx.doi.org/10.3389/fpls.2014.00760 Text en Copyright © 2015 Zhao, Lu, Zhang, Wu, Yang and Wu. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Zhao, Linmao Lu, Jingxia Zhang, Jianxia Wu, Pei-Ying Yang, Songguang Wu, Keqiang |
spellingShingle |
Zhao, Linmao Lu, Jingxia Zhang, Jianxia Wu, Pei-Ying Yang, Songguang Wu, Keqiang Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum) |
author_facet |
Zhao, Linmao Lu, Jingxia Zhang, Jianxia Wu, Pei-Ying Yang, Songguang Wu, Keqiang |
author_sort |
Zhao, Linmao |
title |
Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum) |
title_short |
Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum) |
title_full |
Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum) |
title_fullStr |
Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum) |
title_full_unstemmed |
Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum) |
title_sort |
identification and characterization of histone deacetylases in tomato (solanum lycopersicum) |
description |
Histone acetylation and deacetylation at the N-terminus of histone tails play crucial roles in the regulation of eukaryotic gene activity. Histone acetylation and deacetylation are catalyzed by histone acetyltransferases and histone deacetylases (HDACs), respectively. A growing number of studies have demonstrated the importance of histone deacetylation/acetylation on genome stability, transcriptional regulation, development and response to stress in Arabidopsis. However, the biological functions of HDACs in tomato have not been investigated previously. Fifteen HDACs identified from tomato (Solanum lycopersicum) can be grouped into RPD3/HDA1, SIR2 and HD2 families based on phylogenetic analysis. Meanwhile, 10 members of the RPD3/HDA1 family can be further subdivided into four groups, namely Class I, Class II, Class III, and Class IV. High similarities of protein sequences and conserved domains were identified among SlHDACs and their homologs in Arabidopsis. Most SlHDACs were expressed in all tissues examined with different transcript abundance. Transient expression in Arabidopsis protoplasts showed that SlHDA8, SlHDA1, SlHDA5, SlSRT1 and members of the HD2 family were localized to the nucleus, whereas SlHDA3 and SlHDA4 were localized in both the cytoplasm and nucleus. The difference in the expression patterns and subcellular localization of SlHDACs suggest that they may play distinct functions in tomato. Furthermore, we found that three members of the RPD3/HDA1 family, SlHDA1, SIHDA3 and SlHDA4, interacted with TAG1 (TOMATO AGAMOUS1) and TM29 (TOMATO MADS BOX29), two MADS-box proteins associated with tomato reproductive development, indicating that these HDACs may be involved in gene regulation in reproductive development. |
publisher |
Frontiers Media S.A. |
publishDate |
2015 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4285013/ |
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1613173627092467712 |