Relevant bibliographies by topics / Phosphorylation of histone H3 at threonine 3

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Academic literature on the topic 'Phosphorylation of histone H3 at threonine 3'

Author: Grafiati
Published: 25 May 2024

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Journal articles on the topic "Phosphorylation of histone H3 at threonine 3"

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Polioudaki, Hara, Yolanda Markaki, Niki Kourmouli, George Dialynas, Panayiotis A. Theodoropoulos, Prim B. Singh, and Spyros D. Georgatos. "Mitotic phosphorylation of histone H3 at threonine 3." FEBS Letters 560, no. 1-3 (February 4, 2004): 39–44. http://dx.doi.org/10.1016/s0014-5793(04)00060-2.

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Hurd, Paul J., Andrew J. Bannister, Karen Halls, Mark A. Dawson, Michiel Vermeulen, Jesper V. Olsen, Heba Ismail, et al. "Phosphorylation of Histone H3 Thr-45 Is Linked to Apoptosis." Journal of Biological Chemistry 284, no. 24 (April 10, 2009): 16575–83. http://dx.doi.org/10.1074/jbc.m109.005421.

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Numerous post-translational modifications have been identified in histones. Most of these occur within the histone tails, but a few have been identified within the histone core sequences. Histone core post-translational modifications have the potential to directly modulate nucleosome structure and consequently DNA accessibility. Here, we identify threonine 45 of histone H3 (H3T45) as a site of phosphorylation in vivo. We find that phosphorylation of H3T45 (H3T45ph) increases dramatically in apoptotic cells, around the time of DNA nicking. To further explore this connection, we analyzed human neutrophil cells because they are short-lived cells that undergo apoptosis in vivo. Freshly isolated neutrophils contain very little H3T45ph, whereas cells cultured for 20 h possess significant amounts; the kinetics of H3T45ph induction closely parallel those of caspase-3 activation. Cytokine inhibition of neutrophil apoptosis leads to reduced levels of H3T45ph. We identify protein kinase C-δ as the kinase responsible for H3T45ph in vitro and in vivo. Given the nucleosomal position of H3T45, we postulate that H3T45ph induces structural change within the nucleosome to facilitate DNA nicking and/or fragmentation.
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Wang, Zhen, Juan Armando Casas-Mollano, Jianping Xu, Jean-Jack M. Riethoven, Chi Zhang, and Heriberto Cerutti. "Osmotic stress induces phosphorylation of histone H3 at threonine 3 in pericentromeric regions of Arabidopsis thaliana." Proceedings of the National Academy of Sciences 112, no. 27 (June 22, 2015): 8487–92. http://dx.doi.org/10.1073/pnas.1423325112.

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Histone phosphorylation plays key roles in stress-induced transcriptional reprogramming in metazoans but its function(s) in land plants has remained relatively unexplored. Here we report that an Arabidopsis mutant defective in At3g03940 and At5g18190, encoding closely related Ser/Thr protein kinases, shows pleiotropic phenotypes including dwarfism and hypersensitivity to osmotic/salt stress. The double mutant has reduced global levels of phosphorylated histone H3 threonine 3 (H3T3ph), which are not enhanced, unlike the response in the wild type, by drought-like treatments. Genome-wide analyses revealed increased H3T3ph, slight enhancement in trimethylated histone H3 lysine 4 (H3K4me3), and a modest decrease in histone H3 occupancy in pericentromeric/knob regions of wild-type plants under osmotic stress. However, despite these changes in heterochromatin, transposons and repeats remained transcriptionally repressed. In contrast, this reorganization of heterochromatin was mostly absent in the double mutant, which exhibited lower H3T3ph levels in pericentromeric regions even under normal environmental conditions. Interestingly, within actively transcribed protein-coding genes, H3T3ph density was minimal in 5′ genic regions, coincidental with a peak of H3K4me3 accumulation. This pattern was not affected in the double mutant, implying the existence of additional H3T3 protein kinases in Arabidopsis. Our results suggest that At3g03940 and At5g18190 are involved in the phosphorylation of H3T3 in pericentromeric/knob regions and that this repressive epigenetic mark may be important for maintaining proper heterochromatic organization and, possibly, chromosome function(s).
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Żabka, Aneta, Natalia Gocek, Konrad Winnicki, Paweł Szczeblewski, Tomasz Laskowski, and Justyna Teresa Polit. "Changes in Epigenetic Patterns Related to DNA Replication in Vicia faba Root Meristem Cells under Cadmium-Induced Stress Conditions." Cells 10, no. 12 (December 3, 2021): 3409. http://dx.doi.org/10.3390/cells10123409.

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Experiments on Vicia faba root meristem cells exposed to 150 µM cadmium chloride (CdCl2) were undertaken to analyse epigenetic changes, mainly with respect to DNA replication stress. Histone modifications examined by means of immunofluorescence labeling included: (1) acetylation of histone H3 on lysine 56 (H3K56Ac), involved in transcription, S phase, and response to DNA damage during DNA biosynthesis; (2) dimethylation of histone H3 on lysine 79 (H3K79Me2), correlated with the replication initiation; (3) phosphorylation of histone H3 on threonine 45 (H3T45Ph), engaged in DNA synthesis and apoptosis. Moreover, immunostaining using specific antibodies against 5-MetC-modified DNA was used to determine the level of DNA methylation. A significant decrease in the level of H3K79Me2, noted in all phases of the CdCl2-treated interphase cell nuclei, was found to correspond with: (1) an increase in the mean number of intranuclear foci of H3K56Ac histones (observed mainly in S-phase), (2) a plethora of nuclear and nucleolar labeling patterns (combined with a general decrease in H3T45Ph), and (3) a decrease in DNA methylation. All these changes correlate well with a general viewpoint that DNA modifications and post-translational histone modifications play an important role in gene expression and plant development under cadmium-induced stress conditions.
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Yoshida, Makoto M., Lily Ting, Steven P. Gygi, and Yoshiaki Azuma. "SUMOylation of DNA topoisomerase IIα regulates histone H3 kinase Haspin and H3 phosphorylation in mitosis." Journal of Cell Biology 213, no. 6 (June 20, 2016): 665–78. http://dx.doi.org/10.1083/jcb.201511079.

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DNA topoisomerase II (TOP2) plays a pivotal role in faithful chromosome separation through its strand-passaging activity that resolves tangled genomic DNA during mitosis. Additionally, TOP2 controls progression of mitosis by activating cell cycle checkpoints. Recent work showed that the enzymatically inert C-terminal domain (CTD) of TOP2 and its posttranslational modification are critical to this checkpoint regulation. However, the molecular mechanism has not yet been determined. By using Xenopus laevis egg extract, we found that SUMOylation of DNA topoisomerase IIα (TOP2A) CTD regulates the localization of the histone H3 kinase Haspin and phosphorylation of histone H3 at threonine 3 at the centromere, two steps known to be involved in the recruitment of the chromosomal passenger complex (CPC) to kinetochores in mitosis. Robust centromeric Haspin localization requires SUMOylated TOP2A CTD binding activity through SUMO-interaction motifs and the phosphorylation of Haspin. We propose a novel mechanism through which the TOP2 CTD regulates the CPC via direct interaction with Haspin at mitotic centromeres.
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Karakkat, Jimsheena V., Suneesh Kaimala, Sreejisha P. Sreedharan, Princy Jayaprakash, Ernest A. Adeghate, Suraiya A. Ansari, Ernesto Guccione, Eric P. K. Mensah-Brown, and Bright Starling Emerald. "The metabolic sensor PASK is a histone 3 kinase that also regulates H3K4 methylation by associating with H3K4 MLL2 methyltransferase complex." Nucleic Acids Research 47, no. 19 (September 16, 2019): 10086–103. http://dx.doi.org/10.1093/nar/gkz786.

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Abstract The metabolic sensor Per-Arnt-Sim (Pas) domain-containing serine/threonine kinase (PASK) is expressed predominantly in the cytoplasm of different cell types, although a small percentage is also expressed in the nucleus. Herein, we show that the nuclear PASK associates with the mammalian H3K4 MLL2 methyltransferase complex and enhances H3K4 di- and tri-methylation. We also show that PASK is a histone kinase that phosphorylates H3 at T3, T6, S10 and T11. Taken together, these results suggest that PASK regulates two different H3 tail modifications involving H3K4 methylation and H3 phosphorylation. Using muscle satellite cell differentiation and functional analysis after loss or gain of Pask expression using the CRISPR/Cas9 system, we provide evidence that some of the regulatory functions of PASK during development and differentiation may occur through the regulation of these histone modifications.
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Kang, Hyoeun, Yong Seok Park, Dong-Hyung Cho, Jae-Sung Kim, and Jeong Su Oh. "Dynamics of histone H3 phosphorylation at threonine 3 during meiotic maturation in mouse oocytes." Biochemical and Biophysical Research Communications 458, no. 2 (March 2015): 280–86. http://dx.doi.org/10.1016/j.bbrc.2015.01.099.

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Wang, Fangwei, Natalia P. Ulyanova, John R. Daum, Debasis Patnaik, Anna V. Kateneva, Gary J. Gorbsky, and Jonathan M. G. Higgins. "Haspin inhibitors reveal centromeric functions of Aurora B in chromosome segregation." Journal of Cell Biology 199, no. 2 (October 15, 2012): 251–68. http://dx.doi.org/10.1083/jcb.201205106.

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Haspin phosphorylates histone H3 at threonine-3 (H3T3ph), providing a docking site for the Aurora B complex at centromeres. Aurora B functions to correct improper kinetochore–microtubule attachments and alert the spindle checkpoint to the presence of misaligned chromosomes. We show that Haspin inhibitors decreased H3T3ph, resulting in loss of centromeric Aurora B and reduced phosphorylation of centromere and kinetochore Aurora B substrates. Consequently, metaphase chromosome alignment and spindle checkpoint signaling were compromised. These effects were phenocopied by microinjection of anti-H3T3ph antibodies. Retargeting Aurora B to centromeres partially restored checkpoint signaling and Aurora B–dependent phosphorylation at centromeres and kinetochores, bypassing the need for Haspin activity. Haspin inhibitors did not obviously affect phosphorylation of histone H3 at serine-10 (H3S10ph) by Aurora B on chromosome arms but, in Aurora B reactivation assays, recovery of H3S10ph was delayed. Haspin inhibitors did not block Aurora B localization to the spindle midzone in anaphase or Aurora B function in cytokinesis. Thus, Haspin inhibitors reveal centromeric roles of Aurora B in chromosome movement and spindle checkpoint signaling.
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Quadri, Roberto, Sarah Sertic, Anna Ghilardi, Diego Rondelli, Guido Roberto Gallo, Luca Del Giacco, and Marco Muzi-Falconi. "Phosphorylation of H3-Thr3 by Haspin Is Required for Primary Cilia Regulation." International Journal of Molecular Sciences 22, no. 14 (July 20, 2021): 7753. http://dx.doi.org/10.3390/ijms22147753.

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Primary cilia are commonly found on most quiescent, terminally differentiated cells and play a major role in the regulation of the cell cycle, cell motility, sensing, and cell–cell communication. Alterations in ciliogenesis and cilia maintenance are causative of several human diseases, collectively known as ciliopathies. A key determinant of primary cilia is the histone deacetylase HDAC6, which regulates their length and resorption and whose distribution is regulated by the death inducer-obliterator 3 (Dido3). Here, we report that the atypical protein kinase Haspin is a key regulator of cilia dynamics. Cells defective in Haspin activity exhibit longer primary cilia and a strong delay in cilia resorption upon cell cycle reentry. We show that Haspin is active in quiescent cells, where it phosphorylates threonine 3 of histone H3, a known mitotic Haspin substrate. Forcing Dido3 detachment from the chromatin prevents Haspin inhibition from impacting cilia dynamics, suggesting that Haspin activity is required for the relocalization of Dido3–HDAC6 to the basal body. Exploiting the zebrafish model, we confirmed the physiological relevance of this mechanism. Our observations shed light on a novel player, Haspin, in the mechanisms that govern the determination of cilia length and the homeostasis of mature cilia.
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Nguyen, A. L., A. S. Gentilello, A. Z. Balboula, V. Shrivastava, J. Ohring, and K. Schindler. "Phosphorylation of threonine 3 on histone H3 by haspin kinase is required for meiosis I in mouse oocytes." Journal of Cell Science 127, no. 23 (October 14, 2014): 5066–78. http://dx.doi.org/10.1242/jcs.158840.

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Dissertations / Theses on the topic "Phosphorylation of histone H3 at threonine 3"

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Pontheaux, Florian. "Activité traductionnelle et dynamique mitotique induites par la fécondation chez l’oursin." Electronic Thesis or Diss., Sorbonne université, 2022. http://www.theses.fr/2022SORUS209.

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La régulation fine de la traduction pour la dynamique du cycle cellulaire est un sujet important dans la recherche cellulaire. Au cours de ma thèse, j'ai analysé les relations entre l’activité traductionnelle des ARNm et les divisions embryonnaires mitotiques d'oursins. La fécondation de l'œuf déclenche l'activation de la machinerie traductionnelle nécessaire à la reprise des divisions mitotiques. Un réseau de régulation traductionnelle (TlRN), indépendant de la transcription, reste à identifier et à caractériser en amont des acteurs du cycle cellulaire. A la recherche d'activités mitotiques pour visualiser la dynamique spatiale à l'intérieur d'œufs, j'ai obtenu des données originales montrant l'activité dynamique et spatiale du complexe mitotique CyclinB/CDK1 et la phosphorylation de l'histone H3 sur la thréonine 3 (pH3T3) pendant la mitose embryonnaire. Ensuite, j'ai analysé le rôle in vivo de 5'UTR spécifiques pour contrôler le recrutement d'ARNm dans les polysomes actifs après la fécondation. Enfin, j'ai montré que la traduction de l'ARNm codant pour eIF4B (facteur d'initiation eucaryote 4B) contrôle l'activité traductionnelle et la dynamique des deux premières divisions mitotiques induites par la fécondation. Je propose qu'eIF4B agisse comme un régulateur positif au sein du TlRN. Ces données permettront d'étudier l'effet potentiel d'eIF4B sur les activités CDK1 et pH3T3
Fine tuning of translation for cell cycle dynamics remains an important topic in cell research. During my thesis, I analyzed the relationships between mRNA translational activity and mitotic cell division using sea urchin embryos. Egg fertilization triggers the activation of the translational machinery, which is required for resuming the first mitotic division, independently of any transcription. A Translational Regulatory Network (TlRN) remains to be identified and characterized upstream of the cell cycle actors. Seeking mitotic activities that can help visualize spatial dynamics inside isolated eggs, I obtained original data showing the spatial and dynamic activity of the mitotic complex CyclinB/CDK1 and the phosphorylation of histone H3 at threonine 3 (pH3T3) during embryonic mitosis. Then, I analyzed the in vivo role of specific 5’UTR for controlling the mRNA recruitment onto active polysome following fertilization. Finally, I showed that the translation of the mRNA encoding for eIF4B (eukaryotic Initiation Factor 4B) controls the translational activity and dynamics of the first two mitotic divisions induced by fertilization. I propose that eIF4B acts as a positive regulator within the TlRN. These data will allow to study the potential effect of eIF4B acting upstream the spatial dynamics of CDK1 and pH3T3 activities
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Book chapters on the topic "Phosphorylation of histone H3 at threonine 3"

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Moraes, Izabel, and Juan Armando Casas-Mollano. "Histone H3 Phosphorylation in Plants and Other Organisms." In Epigenetics in Plants of Agronomic Importance: Fundamentals and Applications, 47–70. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-07971-4_4.

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