GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean

<p>Abstract</p> <p>Background</p> <p>Accumulated evidence suggest that specific patterns of histone posttranslational modifications (PTMs) and their crosstalks may determine transcriptional outcomes. However, the regulatory mechanisms of these "histone codes"...

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Main Authors: Wu Tao, Pi Er-Xu, Tsai Sau-Na, Lam Hon-Ming, Sun Sai-Ming, Kwan Yiu, Ngai Sai-Ming
Format: Article
Language:English
Published: BMC 2011-12-01
Series:BMC Plant Biology
Online Access:http://www.biomedcentral.com/1471-2229/11/178
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spelling doaj-254ac7744ade43f4809ae4e2f26321b02020-11-24T23:29:04ZengBMCBMC Plant Biology1471-22292011-12-0111117810.1186/1471-2229-11-178GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybeanWu TaoPi Er-XuTsai Sau-NaLam Hon-MingSun Sai-MingKwan YiuNgai Sai-Ming<p>Abstract</p> <p>Background</p> <p>Accumulated evidence suggest that specific patterns of histone posttranslational modifications (PTMs) and their crosstalks may determine transcriptional outcomes. However, the regulatory mechanisms of these "histone codes" in plants remain largely unknown.</p> <p>Results</p> <p>In this study, we demonstrate for the first time that a salinity stress inducible PHD (plant homeodomain) finger domain containing protein GmPHD5 can read the "histone code" underlying the methylated H3K4. GmPHD5 interacts with other DNA binding proteins, including GmGNAT1 (an acetyl transferase), GmElongin A (a transcription elongation factor) and GmISWI (a chromatin remodeling protein). Our results suggest that GmPHD5 can recognize specific histone methylated H3K4, with preference to di-methylated H3K4. Here, we illustrate that the interaction between GmPHD5 and GmGNAT1 is regulated by the self-acetylation of GmGNAT1, which can also acetylate histone H3. GmGNAT1 exhibits a preference toward acetylated histone H3K14. These results suggest a histone crosstalk between methylated H3K4 and acetylated H3K14. Consistent to its putative roles in gene regulation under salinity stress, we showed that GmPHD5 can bind to the promoters of some confirmed salinity inducible genes in soybean.</p> <p>Conclusion</p> <p>Here, we propose a model suggesting that the nuclear protein GmPHD5 is capable of regulating the crosstalk between histone methylation and histone acetylation of different lysine residues. Nevertheless, GmPHD5 could also recruit chromatin remodeling factors and transcription factors of salt stress inducible genes to regulate their expression in response to salinity stress.</p> http://www.biomedcentral.com/1471-2229/11/178
collection DOAJ
language English
format Article
sources DOAJ
author Wu Tao
Pi Er-Xu
Tsai Sau-Na
Lam Hon-Ming
Sun Sai-Ming
Kwan Yiu
Ngai Sai-Ming
spellingShingle Wu Tao
Pi Er-Xu
Tsai Sau-Na
Lam Hon-Ming
Sun Sai-Ming
Kwan Yiu
Ngai Sai-Ming
GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean
BMC Plant Biology
author_facet Wu Tao
Pi Er-Xu
Tsai Sau-Na
Lam Hon-Ming
Sun Sai-Ming
Kwan Yiu
Ngai Sai-Ming
author_sort Wu Tao
title GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean
title_short GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean
title_full GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean
title_fullStr GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean
title_full_unstemmed GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean
title_sort gmphd5 acts as an important regulator for crosstalk between histone h3k4 di-methylation and h3k14 acetylation in response to salinity stress in soybean
publisher BMC
series BMC Plant Biology
issn 1471-2229
publishDate 2011-12-01
description <p>Abstract</p> <p>Background</p> <p>Accumulated evidence suggest that specific patterns of histone posttranslational modifications (PTMs) and their crosstalks may determine transcriptional outcomes. However, the regulatory mechanisms of these "histone codes" in plants remain largely unknown.</p> <p>Results</p> <p>In this study, we demonstrate for the first time that a salinity stress inducible PHD (plant homeodomain) finger domain containing protein GmPHD5 can read the "histone code" underlying the methylated H3K4. GmPHD5 interacts with other DNA binding proteins, including GmGNAT1 (an acetyl transferase), GmElongin A (a transcription elongation factor) and GmISWI (a chromatin remodeling protein). Our results suggest that GmPHD5 can recognize specific histone methylated H3K4, with preference to di-methylated H3K4. Here, we illustrate that the interaction between GmPHD5 and GmGNAT1 is regulated by the self-acetylation of GmGNAT1, which can also acetylate histone H3. GmGNAT1 exhibits a preference toward acetylated histone H3K14. These results suggest a histone crosstalk between methylated H3K4 and acetylated H3K14. Consistent to its putative roles in gene regulation under salinity stress, we showed that GmPHD5 can bind to the promoters of some confirmed salinity inducible genes in soybean.</p> <p>Conclusion</p> <p>Here, we propose a model suggesting that the nuclear protein GmPHD5 is capable of regulating the crosstalk between histone methylation and histone acetylation of different lysine residues. Nevertheless, GmPHD5 could also recruit chromatin remodeling factors and transcription factors of salt stress inducible genes to regulate their expression in response to salinity stress.</p>
url http://www.biomedcentral.com/1471-2229/11/178
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