ArticleBMC plant biology2012
Histone acetyltransferases in rice (Oryza sativa L.): phylogenetic analysis, subcellular localization and expression.
Article in BMC plant biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 147 citations in OpenAlex.
- Histone acetyltransferases as integrative epigenetic regulators of plant abiotic stress responses.Plant cell reports · 2026Review
- Regulatory role of epigenetics in rice immunity against bacterial and fungal pathogens.Crop health · 2026Review
- Targeting histone acetylation to enhance somatic embryogenesis in Quercus suber L.Tree physiology · 2025Article
- Transcriptional and epigenomic changes in response to polyethylene glycol-triggered osmotic stress in Brassica napus L.Journal of experimental botany · 2025Article
- Histone acetyltransferase HAF2 associates with pyruvate dehydrogenase complex to control H3K14ac and H3K23ac in ethylene response.Cell reports · 2025Article
- Genetic and Genomic Tools in Breeding for Resistance to Fusarium Stalk Rot in Maize (Plants (Basel, Switzerland) · 2025Review
- Roles of Histone Acetylation and Deacetylation in Root Development.Plants (Basel, Switzerland) · 2024Review
- Unveiling the role of epigenetics in leaf senescence: a comparative study to identify different epigenetic regulations of senescence types in barley leaves.BMC plant biology · 2024Article
- Advances in understanding the roles of plant HAT and HDAC in non-histone protein acetylation and deacetylation.Planta · 2024Review
- Systematic Analysis of theInternational journal of molecular sciences · 2024Article
- Research Progress on the Mechanism and Function of Histone Acetylation Regulating the Interaction between Pathogenic Fungi and Plant Hosts.Journal of fungi (Basel, Switzerland) · 2024Review
- Genome-wide identification and expression analysis of histone deacetylase and histone acetyltransferase genes in response to drought in poplars.BMC genomics · 2024Article
- Recent advancements in the role of histone acetylation dynamics to improve stress responses in plants.Molecular biology reports · 2024Review
- Article
- Regulation of Disease-Resistance Genes against CWMV Infection by NbHAG1-Mediated H3K36ac.International journal of molecular sciences · 2024Article
- Rice responds to Spodoptera frugiperda infestation via epigenetic regulation of H3K9ac in the jasmonic acid signaling and phenylpropanoid biosynthesis pathways.Plant cell reports · 2024Article
- Plant responses to abiotic stress regulated by histone acetylation.Frontiers in plant science · 2024Review
- Identification of the histone acetyltransferase gene family in theFrontiers in plant science · 2024Article
- ACL and HAT1 form a nuclear module to acetylate histone H4K5 and promote cell proliferation.Nature communications · 2023Article
- Identification of histone acetyltransferase genes responsible for cannabinoid synthesis in hemp.Chinese medicine · 2023Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundHistone acetyltransferases (HATs) play an important role in eukaryotic transcription. Eight HATs identified in rice (OsHATs) can be organized into four families, namely the CBP (OsHAC701, OsHAC703, and OsHAC704), TAFII250 (OsHAF701), GNAT (OsHAG702, OsHAG703, and OsHAG704), and MYST (OsHAM701) families. The biological functions of HATs in rice remain unknown, so a comprehensive protein sequence analysis of the HAT families was conducted to investigate their potential functions. In addition, the subcellular localization and expression patterns of the eight OsHATs were analyzed.
resultsOn the basis of a phylogenetic and domain analysis, monocotyledonous CBP family proteins can be subdivided into two groups, namely Group I and Group II. Similarly, dicotyledonous CBP family proteins can be divided into two groups, namely Group A and Group B. High similarities of protein sequences, conserved domains and three-dimensional models were identified among OsHATs and their homologs in Arabidopsis thaliana and maize. Subcellular localization predictions indicated that all OsHATs might localize in both the nucleus and cytosol. Transient expression in Arabidopsis protoplasts confirmed the nuclear and cytosolic localization of OsHAC701, OsHAG702, and OsHAG704. Real-time quantitative polymerase chain reaction analysis demonstrated that the eight OsHATs were expressed in all tissues examined with significant differences in transcript abundance, and their expression was modulated by abscisic acid and salicylic acid as well as abiotic factors such as salt, cold, and heat stresses.
conclusionsBoth monocotyledonous and dicotyledonous CBP family proteins can be divided into two distinct groups, which suggest the possibility of functional diversification. The high similarities of protein sequences, conserved domains and three-dimensional models among OsHATs and their homologs in Arabidopsis and maize suggested that OsHATs have multiple functions. OsHAC701, OsHAG702, and OsHAG704 were localized in both the nucleus and cytosol in transient expression analyses with Arabidopsis protoplasts. OsHATs were expressed constitutively in rice, and their expression was regulated by exogenous hormones and abiotic stresses, which suggested that OsHATs may play important roles in plant defense responses.
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