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

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About: GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean
Creator	Lam, Hon-Ming Ngai, Sai-Ming Pi, Er-Xu Sun, Sai-Ming Tsai, Sau-Na Wu, Tao Kwan, Yiu
Source	Medline; PMC
abstract	BACKGROUND: Accumulated evidence suggest that specific patterns of histone posttranslational modifications (PTMs) and their crosstalks may determine transcriptional outcomes. However, the regulatory mechanisms of these %22histone codes%22 in plants remain largely unknown. RESULTS: 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 %22histone code%22 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. CONCLUSION: 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.
has issue date	2011-12-15(xsd:dateTime)
bibo:doi	10.1186/1471-2229-11-178
bibo:pmid	22168212
has license	cc-by
sha1sum (hex)	6f62efb20f820241aeb1a8e16af68502fedc9b43
schema:url	https://doi.org/10.1186/1471-2229-11-178
resource representing a document's title	GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean
has PubMed Central identifier	PMC3288756
has PubMed identifier	22168212
schema:publication	BMC Plant Biol
resource representing a document's body	covid:6f62efb20f820241aeb1a8e16af68502fedc9b43#body_text
is schema:about of	named entity 'DI-METHYLATION' named entity 'acetylation' named entity 'HISTONE' named entity 'REGULATORY' named entity 'THEIR' named entity 'UNKNOWN' named entity 'DETERMINE' named entity 'SUGGEST' named entity 'MECHANISMS' named entity 'THESE' named entity 'POSTTRANSLATIONAL' named entity 'PLANTS' named entity 'OUTCOMES' named entity 'SPECIFIC' named entity 'H3K14 ACETYLATION' named entity 'EVIDENCE' covid:arg/6f62efb20f820241aeb1a8e16af68502fedc9b43 named entity 'REGULATOR' named entity 'RESPONSE TO SALINITY' named entity 'IMPORTANT' named entity 'ACTS' named entity 'SALINITY STRESS' named entity 'CROSSTALK' named entity 'LARGELY' named entity 'ACCUMULATED' named entity 'TRANSCRIPTIONAL' named entity 'HISTONE' named entity 'SOYBEAN' named entity 'H3K4' named entity 'CODES' named entity 'BACKGROUND' named entity 'PATTERNS' named entity 'posttranslational modifications' named entity 'histone' named entity 'stress' named entity 'transcriptional' named entity 'soybean' named entity 'Chinese University of Hong Kong' named entity 'Perkin Elmer' named entity 'histone modifications' named entity 'nuclear proteins' named entity 'solid-phase peptide synthesis' named entity 'PMSF' named entity 'peptide' named entity 'primer' named entity 'antibody' named entity 'nucleosome' named entity 'methylated' named entity 'histone' named entity 'interact' named entity 'soybean' named entity 'stained with silver' named entity 'PHD finger' named entity 'soybean' named entity 'methylated' named entity 'PMSF' named entity 'optical density' named entity 'S1C' named entity 'PCR' named entity 'cDNA' named entity 'methylated' named entity 'EDTA' named entity 'Millipore' named entity 'antibodies' named entity 'Antibodies' named entity 'protein' named entity 'antibody' named entity 'Western blotting' named entity 'protein' named entity 'low affinity' named entity 'methylated' named entity 'protein' named entity 'antibody' named entity 'nuclei' named entity 'methylated'

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