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11دورية أكاديمية
المساهمون: Ho-Geun Yoon, Doug W. Chan, Jiemin Wong, Jun Qin, Albert B. Reynolds, Yoon, Ho Geun
مصطلحات موضوعية: Animals, Carrier Proteins/genetics, Carrier Proteins/metabolism, CpG Islands/genetics, DNA Methylation, DNA-Binding Proteins/genetics, DNA-Binding Proteins/metabolism, DNA-Cytosine Methylases/genetics, DNA-Cytosine Methylases/metabolism, Eukaryotic Cells/metabolism, Genes, Regulator/genetics, HeLa Cells, Histone Deacetylases/genetics, Histone Deacetylases/metabolism, Histones/genetics, Histones/metabolism, Humans, Lysine/genetics, Lysine/metabolism, Nuclear Proteins/genetics, Nuclear Proteins/metabolism, Nuclear Receptor Co-Repressor 1, Promoter Regions, Genetic/genetics, Repressor Proteins/genetics, Repressor Proteins/metabolism, Transcription Factors/genetics, Transcription Factors/metabolism
الوقت: 14527417
الوصف: The identification and characterization of molecular mechanisms utilized by cells to mediate transcriptional repression at methylated loci are fundamental to understanding the biological consequences of DNA methylation. Here we demonstrate that Kaiso, a methyl CpG binding protein belonging to the BTB/POZ family of transcription factors, is a component of the human N-CoR complex. In vitro, the Kaiso/N-CoR complex binds specific CpG-rich sequences in a methylation-dependent manner. In vivo, Kaiso targets the N-CoR complex to the MTA2 gene promoter in a methylation-dependent manner. Importantly, we demonstrate that Kaiso is required for transcriptional repression of the methylated MTA2 locus. Furthermore, this repression also requires a functional N-CoR deacetylase complex, which brings about histone hypoacetylation and methylation of H3 lysine 9 to the MTA2 locus. Thus, our data demonstrate a critical role for a methyl CpG binding protein in mediating DNA methylation-dependent repression and reveal the mechanism by which it represses transcription. ; open
وصف الملف: 723~734
العلاقة: MOLECULAR CELL; J02256; OAK-2003-00144; https://ir.ymlib.yonsei.ac.kr/handle/22282913/113304Test; http://www.sciencedirect.com/science/article/pii/S1097276503003174Test; T200302514; MOLECULAR CELL, Vol.12(3) : 723-734, 2003
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12
المصدر: EMBO molecular medicine. 11(9)
مصطلحات موضوعية: Histone Deacetylases/genetics, Longevity/drug effects, Genetic, Histone Deacetylase Inhibitors/administration & dosage, Animals, Drug Evaluation, Humans, Preclinical, Healthy Aging/drug effects, Epigenesis
الوصف: Reversing or slowing the aging process brings great promise to treat or prevent age-related disease, and targeting the hallmarks of aging is a strategy to achieve this. Epigenetics affects several if not all of the hallmarks of aging and has therefore emerged as a central target for intervention. One component of epigenetic regulation involves histone deacetylases (HDAC), which include the “classical” histone deacetylases (of class I, II, and IV) and sirtuin deacetylases (of class III). While targeting sirtuins for healthy aging has been extensively reviewed elsewhere, this review focuses on pharmacologically inhibiting the classical HDACs to promote health and longevity. We describe the theories of how classical HDAC inhibitors may operate to increase lifespan, supported by studies in model organisms. Furthermore, we explore potential mechanisms of how HDAC inhibitors may have such a strong grasp on health and longevity, summarizing their links to other hallmarks of aging. Finally, we show the wide range of age-related preclinical disease models, ranging from neurodegeneration to heart disease, diabetes to sarcopenia, which show improvement upon HDAC inhibition.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=dris___00893::d6a1a426b7c561dd686ba9fed4c0d1beTest
https://doi.org/10.15252/emmm.201809854Test -
13
المؤلفون: A. Rasim Barutcu, Laura Pölsler, Yvette Wefeld-Neuenfeld, Philipp G. Maass, Atakan Aydin, Katharina Rittscher, Thomas Liehr, Julia Lichtenwald, Sigrid Tinschert, Sylvia Bähring, Anja Weise, Friedrich C. Luft, John L. Rinn
المساهمون: Medical Genetics
المصدر: The EMBO Journal. 37
مصطلحات موضوعية: Interphase/genetics, 0301 basic medicine, Cell type, Cell Nucleus/genetics, Biology, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Chromosomes, Human, Pair 17/genetics, medicine, Humans, Chromosomes, Human, Pair 2/genetics, Molecular Biology, In Situ Hybridization, Fluorescence, Chromosome 12, Genetics, Chromosomes, Human, Pair 12/genetics, Histone Deacetylases/genetics, Repressor Proteins/genetics, General Immunology and Microbiology, Mesenchymal Stem Cells/cytology, General Neuroscience, Mesenchymal stem cell, Chromosome, Karyotype, Translocation, Genetic/genetics, HDAC4, 030104 developmental biology, medicine.anatomical_structure, Interphase, Chromosome Deletion, Nucleus, Gene Deletion
الوصف: Chromosomes occupy distinct interphase territories in the three-dimensional nucleus. However, how these chromosome territories are arranged relative to one another is poorly understood. Here, we investigated the inter-chromosomal interactions between chromosomes 2q, 12, and 17 in human mesenchymal stem cells (MSCs) and MSC-derived cell types by DNA-FISH We compared our findings in normal karyotypes with a three-generation family harboring a 2q37-deletion syndrome, featuring a heterozygous partial deletion of histone deacetylase 4 (HDAC4) on chr2q37. In normal karyotypes, we detected stable, recurring arrangements and interactions between the three chromosomal territories with a tissue-specific interaction bias at certain loci. These inter-chromosomal interactions were confirmed by Hi-C. Interestingly, the disease-related HDAC4 deletion resulted in displaced inter-chromosomal arrangements and altered interactions between the deletion-affected chromosome 2 and chromosome 12 and/or 17 in 2q37-deletion syndrome patients. Our findings provide evidence for a direct link between a structural chromosomal aberration and altered interphase architecture that results in a nuclear configuration, supporting a possible molecular pathogenesis.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95b0d29c3b3acb595fda03dee414610fTest
https://doi.org/10.15252/embj.201696257Test -
14
المؤلفون: Raymond J. Pierce, Wolfgang Sippl, Julien Lancelot, Karin Schmidtkunz, Alokta Chakrabarti, Dina Robaa, Jelena Melesina, Tajith B. Shaik, Christophe Romier, Conrad V. Simoben, Manfred Jung, Srinivasaraghavan Kannan, Martin Marek
المساهمون: Romier, Christophe, Martin-Luther-Universität Halle Wittenberg (MLU), Albert-Ludwigs-Universität Freiburg, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), This work and the authors of this article received funding from the European Union’s Seventh Framework Programme for Research, Technological Development and Demonstration under Grant Agreements 241865 (SEtTReND) and 602080 (A-ParaDDisE). Further support was received by the Deutsche Forschungsgemeinschaft (Ju-295/13-1, SI-868/13-1). MM, TBS and CR are supported by institutional funds from the Centre National de la Recherche Scientifique (CNRS), the Institut National de la Santé et de la Recherche Médicale (INSERM) and the Université de Strasbourg., The authors acknowledge the support and the use of resources of the French Infrastructure for Integrated Structural Biology FRISBI ANR-10-INBS-05 and of Instruct-ERIC. We wish to thank members of the ESRF-EMBL joint structural biology groups and the SOLEIL synchrotron for the use of their beamline facilities and for help during data collection. We are grateful to Pierre Legrand (SOLEIL) for his kind assistance for data processing, Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)
المصدر: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
Molecules
Molecules, 2018, 23 (3), pp.566. ⟨10.3390/molecules23030566⟩
Molecules, Vol 23, Iss 3, p 566 (2018)
Molecules; Volume 23; Issue 3; Pages: 566
Molecules, MDPI, 2018, 23 (3), pp.566. ⟨10.3390/molecules23030566⟩مصطلحات موضوعية: 0301 basic medicine, Pyrrolidines, MESH: Helminth Proteins/metabolism, MESH: Histone Deacetylases/metabolism, MESH: Histone Deacetylases/genetics, Pharmaceutical Science, MESH: Protein Structure, Secondary, Gene Expression, Apoptosis, Crystallography, X-Ray, Hydroxamic Acids, Molecular Docking Simulation, MESH: Helminth Proteins/antagonists & inhibitors, MESH: Chelating Agents/chemical synthesis, Protein Structure, Secondary, Analytical Chemistry, 0302 clinical medicine, MESH: Structure-Activity Relationship, MESH: Hydroxamic Acids/chemical synthesis, Drug Discovery, MESH: Zinc/metabolism, MESH: Animals, [SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], MESH: Histone Deacetylase Inhibitors/pharmacology, Chelating Agents, Anthelmintics, biology, Chemistry, MESH: Anthelmintics/pharmacology, Helminth Proteins, Schistosoma mansoni, epigenetics, crystal structure, docking, histone deacetylase (HDAC) inhibitors, schistosomiasis, virtual screening, MESH: Histone Deacetylases/chemistry, 3. Good health, MESH: Schistosoma mansoni/drug effects, MESH: Pyrrolidines/pharmacology, Zinc, Biochemistry, Chemistry (miscellaneous), Molecular Medicine, Protein Binding, MESH: Apoptosis/drug effects, MESH: Gene Expression, In silico, 030231 tropical medicine, MESH: Zinc/chemistry, Article, Histone Deacetylases, lcsh:QD241-441, 03 medical and health sciences, Structure-Activity Relationship, lcsh:Organic chemistry, MESH: Molecular Docking Simulation, Structure–activity relationship, MESH: Protein Binding, Animals, MESH: Helminth Proteins/genetics, Protein Interaction Domains and Motifs, Physical and Theoretical Chemistry, MESH: Histone Deacetylase Inhibitors/chemical synthesis, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Virtual screening, MESH: Protein Interaction Domains and Motifs, Binding Sites, Organic Chemistry, MESH: Hydroxamic Acids/pharmacology, HDAC8, MESH: Schistosoma mansoni/growth & development, Epigenome, biology.organism_classification, MESH: Crystallography, X-Ray, MESH: Anthelmintics/chemical synthesis, Histone Deacetylase Inhibitors, 030104 developmental biology, MESH: Binding Sites, Docking (molecular), MESH: Chelating Agents/pharmacology, MESH: Schistosoma mansoni/enzymology, MESH: Helminth Proteins/chemistry, MESH: Schistosoma mansoni/genetics, MESH: Pyrrolidines/chemical synthesis
الوصف: International audience; A promising means in the search of new small molecules for the treatment of schistosomiasis (amongst other parasitic ailments) is by targeting the parasitic epigenome. In the present study, a docking based virtual screening procedure using the crystal structure of histone deacetylase 8 from Schistosoma mansoni (smHDAC8) was designed. From the developed screening protocol, we were able to identify eight novel N-(2,5-dioxopyrrolidin-3-yl)-n-alkylhydroxamate derivatives as smHDAC8 inhibitors with IC50 values ranging from 4.4-20.3 µM against smHDAC8. These newly identified inhibitors were further tested against human histone deacetylases (hsHDAC1, 6 and 8), and were found also to be exerting interesting activity against them. In silico prediction of the docking pose of the compounds was confirmed by the resolved crystal structure of one of the identified hits. This confirmed these compounds were able to chelate the catalytic zinc ion in a bidentate fashion, whilst showing an inverted binding mode of the hydroxamate group when compared to the reported smHDAC8/hydroxamates crystal structures. Therefore, they can be considered as new potential scaffold for the development of new smHDAC8 inhibitors by further investigation of their structure-activity relationship.
وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c57756972e5c4439f4e393638be3994bTest
http://europepmc.org/articles/PMC6017931Test -
15دورية أكاديمية
المؤلفون: Anand, C., Garg, R., Ghosh, S., Nagaraja, V.
المصدر: Biochemical and Biophysical Research Communications, vol. 493, no. 3, pp. 1204-1209
مصطلحات موضوعية: Acetylation, Bacterial Proteins/genetics, Bacterial Proteins/metabolism, DNA, Bacterial/chemistry, Bacterial/metabolism, DNA-Binding Proteins/genetics, DNA-Binding Proteins/metabolism, Histone Deacetylases/genetics, Histone Deacetylases/metabolism, Mycobacterium tuberculosis/genetics, Mycobacterium tuberculosis/metabolism, Deacetylation, HU, Nucleoid associated proteins, Rv1151c, Sirtuin
الوصف: Till recently, knowledge about epigenetic regulation in bacterial world confined largely to DNA methylation. Lysine acetylation/deacetylation of histones is a major contributor for chromatin dynamics in eukaryotes. However, little is known about such epigenetic changes brought about by post-translational modifications in bacteria. Here, we describe an example of such mechanism occurring in a histone like protein, HU from Mycobacterium tuberculosis (Mtb). Previously, we demonstrated the interaction and acetylation of Mtb HU (MtHU) by one of the acetyl transferases, Eis. In this work, we demonstrate the deacetylation of acetylated HU (MtHU(Ac)) by Rv1151c, the only Sir2 like protein discovered in Mtb. The DNA binding properties of MtHU are significantly altered upon acetylation but reversed consequent to deacetylation by the deacetylase. Deacetylated HU (MtHU(dAc)) bound to relaxed DNA leading to the formation of looped and dense molecules as compared to open structures formed by its acetylated form. Interaction of MtHU(dAc) with linear DNA modifies its organization leading to formation of highly bridged compact structures while binding of MtHU(Ac) leads to the formation of stiff and straight rods. That a nucleoid associated protein can undergo acetylation/deacetylation to alter its DNA binding and architectural role opens up a new dimension of investigation of epigenetic regulation in mycobacteria.
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/28935371; info:eu-repo/semantics/altIdentifier/eissn/1090-2104; https://serval.unil.ch/notice/serval:BIB_93F9B9A2866ETest; urn:issn:0006-291X
الإتاحة: https://doi.org/10.1016/j.bbrc.2017.09.087Test
https://serval.unil.ch/notice/serval:BIB_93F9B9A2866ETest -
16
المؤلفون: Scott W. Hiebert, Emma De Fabiani, Cinzia Magagnotti, Erika Fiorino, Donatella Caruso, Béatrice Desvergne, Annapaola Andolfo, Maurizio Crestani, Rui Silva, Gaia Cermenati, Nico Mitro, Federica Gilardi, Raffaella Longo, Alessandra Ferrari
المصدر: Nature Communications, Vol 8, Iss 1, Pp 1-17 (2017)
Nature Communications
Nature Communications, vol. 8, no. 1, pp. 93مصطلحات موضوعية: Male, 0301 basic medicine, Adipose Tissue, White, Science, General Physics and Astronomy, Adipose tissue, Adipocytes/physiology, Adipose Tissue, Brown/physiology, Adipose Tissue, White/physiology, Animals, Cell Line, Diet, High-Fat, Gene Expression Regulation/physiology, Gene Silencing, Histone Deacetylases/genetics, Histone Deacetylases/metabolism, Lipid Metabolism, Mice, Mice, Knockout, White adipose tissue, Biology, Histone Deacetylases, Article, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, chemistry.chemical_compound, Adipose Tissue, Brown, Adipocytes, PPARA Gene, Fatty acid synthesis, Multidisciplinary, Fatty acid metabolism, Futile cycle, nutritional and metabolic diseases, food and beverages, Lipid metabolism, General Chemistry, HDAC3, 030104 developmental biology, Gene Expression Regulation, chemistry, Biochemistry, lipids (amino acids, peptides, and proteins), hormones, hormone substitutes, and hormone antagonists
الوصف: White adipose tissue (WAT) can undergo a phenotypic switch, known as browning, in response to environmental stimuli such as cold. Post-translational modifications of histones have been shown to regulate cellular energy metabolism, but their role in white adipose tissue physiology remains incompletely understood. Here we show that histone deacetylase 3 (HDAC3) regulates WAT metabolism and function. Selective ablation of Hdac3 in fat switches the metabolic signature of WAT by activating a futile cycle of de novo fatty acid synthesis and β-oxidation that potentiates WAT oxidative capacity and ultimately supports browning. Specific ablation of Hdac3 in adipose tissue increases acetylation of enhancers in Pparg and Ucp1 genes, and of putative regulatory regions of the Ppara gene. Our results unveil HDAC3 as a regulator of WAT physiology, which acts as a molecular brake that inhibits fatty acid metabolism and WAT browning.
Histone deacetylases, such as HDAC3, have been shown to alter cellular metabolism in various tissues. Here the authors show that HDAC3 regulates WAT metabolism by activating a futile cycle of fatty acid synthesis and oxidation, which supports WAT browning.وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c512383fec48820206bfc3269b78fc0bTest
https://doi.org/10.1038/s41467-017-00182-7Test -
17دورية أكاديمية
المؤلفون: Feng, Peiqiang, Guo, Hailong, Chi, Wei, Chai, Xin, Sun, Xuwu, Xu, Xiumei, Ma, Jinfang, Rochaix, Jean-David, Leister, Dario, Wang, Haiyang, Lu, Congming, Zhang, Lixin
المصدر: ISSN: 0027-8424 ; Proceedings of the National Academy of Sciences, vol. 113, no. 38 (2016) p. 10708-10713.
مصطلحات موضوعية: info:eu-repo/classification/ddc/570, info:eu-repo/classification/ddc/580, Arabidopsis/genetics/growth & development, Arabidopsis Proteins/genetics, Carrier Proteins/genetics, Cell Nucleus/genetics/radiation effects, Chloroplasts/genetics/metabolism, Chromatin/genetics/radiation effects, Flowers/genetics/growth & development/radiation effects, Gene Expression Regulation, Plant/radiation effects, Histone Deacetylases/genetics, Light, MADS Domain Proteins/genetics, PHD Zinc Fingers/genetics, Signal Transduction/genetics
الوصف: Light is a major environmental factor regulating flowering time, thus ensuring reproductive success of higher plants. In contrast to our detailed understanding of light quality and photoperiod mechanisms involved, the molecular basis underlying high light-promoted flowering remains elusive. Here we show that, in Arabidopsis, a chloroplast-derived signal is critical for high light-regulated flowering mediated by the FLOWERING LOCUS C (FLC). We also demonstrate that PTM, a PHD transcription factor involved in chloroplast retrograde signaling, perceives such a signal and mediates transcriptional repression of FLC through recruitment of FVE, a component of the histone deacetylase complex. Thus, our data suggest that chloroplasts function as essential sensors of high light to regulate flowering and adaptive responses by triggering nuclear transcriptional changes at the chromatin level.
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/27601637; https://archive-ouverte.unige.ch/unige:111261Test; unige:111261
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18
المؤلفون: Victor Fernandes Vieira, Sandrine Cornaz, Luisa Cironi, Carlo Fusco, Paolo Provero, Giulia Fregni, Ivan Stamenkovic, Igor Letovanec, Michel Aguet, Tanja Petricevic
المصدر: Scientific Reports
Scientific reports, vol. 6, pp. 22113مصطلحات موضوعية: 0301 basic medicine, Beta-catenin, Oncogene Proteins, Fusion, Blotting, Western, Animals, Axin Protein/genetics, Axin Protein/metabolism, Cell Line, Cell Line, Tumor, Gene Expression Profiling/methods, Histone Deacetylases/genetics, Histone Deacetylases/metabolism, Humans, Mice, Microscopy, Confocal, Oncogene Proteins, Fusion/genetics, Oncogene Proteins, Fusion/metabolism, RNA Interference, Repressor Proteins/genetics, Repressor Proteins/metabolism, Reverse Transcriptase Polymerase Chain Reaction, Sarcoma, Synovial/genetics, Sarcoma, Synovial/metabolism, Sarcoma, Synovial/pathology, TCF Transcription Factors/genetics, TCF Transcription Factors/metabolism, Transcription Factors/genetics, Transcription Factors/metabolism, Wnt Signaling Pathway/genetics, beta Catenin/genetics, beta Catenin/metabolism, TCF/LEF family, Histone Deacetylases, Article, Sarcoma, Synovial, 03 medical and health sciences, Axin Protein, AXIN2, Fusion, Wnt Signaling Pathway, Transcription factor, beta Catenin, Gene Expression Profiling, Repressor Proteins, TCF Transcription Factors, Transcription Factors, Multidisciplinary, Oncogene Proteins, Microscopy, Tumor, Synovial, biology, Blotting, Wnt signaling pathway, LRP6, Sarcoma, LRP5, Fusion protein, 030104 developmental biology, Confocal, biology.protein, Cancer research, Western, Co-Repressor Proteins
الوصف: Expression of the SS18/SYT-SSX fusion protein is believed to underlie the pathogenesis of synovial sarcoma (SS). Recent evidence suggests that deregulation of the Wnt pathway may play an important role in SS but the mechanisms whereby SS18-SSX might affect Wnt signaling remain to be elucidated. Here, we show that SS18/SSX tightly regulates the elevated expression of the key Wnt target AXIN2 in primary SS. SS18-SSX is shown to interact with TCF/LEF, TLE and HDAC but not β-catenin in vivo and to induce Wnt target gene expression by forming a complex containing promoter-bound TCF/LEF and HDAC but lacking β-catenin. Our observations provide a tumor-specific mechanistic basis for Wnt target gene induction in SS that can occur in the absence of Wnt ligand stimulation.
وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60efadcc1928d9d1f484ba21cc89d788Test
https://doi.org/10.1038/srep22113Test -
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المؤلفون: Xuwu Sun, Haiyang Wang, Xiumei Xu, Jinfang Ma, Lixin Zhang, Hailong Guo, Congming Lu, Jean-David Rochaix, Peiqiang Feng, Wei Chi, Dario Leister, Xin Chai
المصدر: Proceedings of the National Academy of Sciences, Vol. 113, No 38 (2016) pp. 10708-10713
مصطلحات موضوعية: 0106 biological sciences, 0301 basic medicine, Carrier Proteins/genetics, Chloroplasts, Chromatin/genetics/radiation effects, Light, Arabidopsis, 01 natural sciences, Gene Expression Regulation, Plant, Flowering Locus C, Arabidopsis/genetics/growth & development, Chloroplasts/genetics/metabolism, Plant/radiation effects, Genetics, Histone Deacetylases/genetics, Multidisciplinary, biology, food and beverages, Biological Sciences, Chromatin, Chloroplast, Arabidopsis Proteins/genetics, ddc:580, Signal Transduction, Flowers/genetics/growth & development/radiation effects, PHD Zinc Fingers/genetics, MADS Domain Proteins, Flowers, Histone Deacetylases, Chromatin remodeling, 03 medical and health sciences, MADS Domain Proteins/genetics, ddc:570, Transcription factor, Cell Nucleus, Arabidopsis Proteins, fungi, biology.organism_classification, 030104 developmental biology, Gene Expression Regulation, Histone deacetylase complex, Retrograde signaling, Signal Transduction/genetics, Cell Nucleus/genetics/radiation effects, Carrier Proteins, PHD Zinc Fingers, Transcription Factors, 010606 plant biology & botany
الوصف: Significance Proper timing of flowering transition is vital for the reproductive success of plants and orchestrated by endogenous and external factors; however, the mechanisms of how plants regulate flowering under high light are not well understood. In this study, we show that promotion of flowering by high light involves the coupling of chloroplast retrograde signals and transcriptional silencing of the floral repressor FLOWERING LOCUS C ( FLC ). In response to high light, a chloroplast envelope-localized transcription factor, PTM, releases its N-terminal fragment through processing to associate with the chromatin remodeler FVE and suppresses FLC transcription. This report describes the molecular basis for a unique intracellular signaling pathway derived from chloroplasts in which plants regulate the developmental timing of the flowering transition.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f79f38ecf505dde84e75748016fe17c0Test
https://archive-ouverte.unige.ch/unige:111261Test -
20دورية أكاديمية
المؤلفون: Li, Da-Qiang, Kumar, Rakesh
المصدر: Biochemistry and Molecular Medicine Faculty Publications
مصطلحات موضوعية: Histone Deacetylases--genetics, Neoplasms--genetics, Repressor Proteins--genetics, Biochemistry, Biophysics, and Structural Biology
العلاقة: https://hsrc.himmelfarb.gwu.edu/smhs_biochem_facpubs/167Test; http://dx.doi.org/10.1016/bs.acr.2015.04.005Test
الإتاحة: https://doi.org/10.1016/bs.acr.2015.04.005Test
https://hsrc.himmelfarb.gwu.edu/smhs_biochem_facpubs/167Test
النص الكامل