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Journal articles on the topic 'Histone post-translational modifications (hPTMs)'

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Author: Grafiati

Published: 9 March 2023

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1

Hu, Qiwen, Casey S. Greene, and Elizabeth A. Heller. "Specific histone modifications associate with alternative exon selection during mammalian development." Nucleic Acids Research 48, no. 9 (April 22, 2020): 4709–24. http://dx.doi.org/10.1093/nar/gkaa248.

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Abstract Alternative splicing (AS) is frequent during early mouse embryonic development. Specific histone post-translational modifications (hPTMs) have been shown to regulate exon splicing by either directly recruiting splice machinery or indirectly modulating transcriptional elongation. In this study, we hypothesized that hPTMs regulate expression of alternatively spliced genes for specific processes during differentiation. To address this notion, we applied an innovative machine learning approach to relate global hPTM enrichment to AS regulation during mammalian tissue development. We found that specific hPTMs, H3K36me3 and H3K4me1, play a role in skipped exon selection among all the tissues and developmental time points examined. In addition, we used iterative random forest model and found that interactions of multiple hPTMs most strongly predicted splicing when they included H3K36me3 and H3K4me1. Collectively, our data demonstrated a link between hPTMs and alternative splicing which will drive further experimental studies on the functional relevance of these modifications to alternative splicing.

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Andonegui-Elguera, Marco A., Rodrigo E. Cáceres-Gutiérrez, Alejandro López-Saavedra, Fernanda Cisneros-Soberanis, Montserrat Justo-Garrido, José Díaz-Chávez, and Luis A. Herrera. "The Roles of Histone Post-Translational Modifications in the Formation and Function of a Mitotic Chromosome." International Journal of Molecular Sciences 23, no. 15 (August 5, 2022): 8704. http://dx.doi.org/10.3390/ijms23158704.

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During mitosis, many cellular structures are organized to segregate the replicated genome to the daughter cells. Chromatin is condensed to shape a mitotic chromosome. A multiprotein complex known as kinetochore is organized on a specific region of each chromosome, the centromere, which is defined by the presence of a histone H3 variant called CENP-A. The cytoskeleton is re-arranged to give rise to the mitotic spindle that binds to kinetochores and leads to the movement of chromosomes. How chromatin regulates different activities during mitosis is not well known. The role of histone post-translational modifications (HPTMs) in mitosis has been recently revealed. Specific HPTMs participate in local compaction during chromosome condensation. On the other hand, HPTMs are involved in CENP-A incorporation in the centromere region, an essential activity to maintain centromere identity. HPTMs also participate in the formation of regulatory protein complexes, such as the chromosomal passenger complex (CPC) and the spindle assembly checkpoint (SAC). Finally, we discuss how HPTMs can be modified by environmental factors and the possible consequences on chromosome segregation and genome stability.

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Ghiani, Lavinia, and Susanna Chiocca. "High Risk-Human Papillomavirus in HNSCC: Present and Future Challenges for Epigenetic Therapies." International Journal of Molecular Sciences 23, no. 7 (March 23, 2022): 3483. http://dx.doi.org/10.3390/ijms23073483.

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Head and Neck Squamous Cell Carcinoma (HNSCC) is a highly heterogeneous group of tumors characterized by an incidence of 650,000 new cases and 350,000 deaths per year worldwide and a male to female ratio of 3:1. The main risk factors are alcohol and tobacco consumption and Human Papillomavirus (HPV) infections. HNSCC cases are divided into two subgroups, the HPV-negative (HPV−) and the HPV-positive (HPV+) which have different clinicopathological and molecular profiles. However, patients are still treated with the same therapeutic regimens. It is thus of utmost importance to characterize the molecular mechanisms underlying these differences to find new biomarkers and novel therapeutic targets towards personalized therapies. Epigenetic alterations are a hallmark of cancer and can be exploited as both promising biomarkers and potential new targets. E6 and E7 HPV oncoviral proteins besides targeting p53 and pRb, impair the expression and the activity of several epigenetic regulators. While alterations in DNA methylation patterns have been well described in HPV+ and HPV− HNSCC, accurate histone post-translational modifications (hPTMs) characterization is still missing. Herein, we aim to provide an updated overview on the impact of HPV on the hPTMs landscape in HNSCC. Moreover, we will also discuss the sex and gender bias in HNSCC and how the epigenetic machinery could be involved in this process, and the importance of taking into account sex and/or gender also in this field.

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Tibana, Ramires, Octávio Franco, Rinaldo Pereira, James Navalta, and Jonato Prestes. "Exercise as an Effective Transgenerational Strategy to Overcome Metabolic Syndrome in the Future Generation: Are We There?" Experimental and Clinical Endocrinology & Diabetes 125, no. 06 (May 11, 2017): 347–52. http://dx.doi.org/10.1055/s-0042-120538.

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AbstractMetabolic syndrome (MetS) consist in a combination of cardiovascular risk factors including elevated blood pressure, dyslipidemia, insulin resistance, hyperglycemia and abdominal obesity. Exercise performed before, during and after pregnancy can exert positive effects to counteract MetS risk factors. Here this review aims to analyze the effects of exercise performed before (fathers and mothers) and after periconception (mothers) by using experimental models and its effects on MetS risk factors in offspring. All selected studies investigated the effects of aerobic exercise before, during and after periconception on MetS risk factors in offspring, while no studies utilizing resistance exercise were found. Exercise performed before, and after periconception exerted preventive effects in the offspring, with regards to MetS risk factors. However, more studies focusing on the dose-response of exercise before, and after periconception may reveal interesting results on MetS risk factor in offspring. Thus, the prevention from chronic degenerative diseases can be improved by mother exercise and might be associated with epigenetic mechanisms, such as DNA methylation, hPTMs (histone post translational modifications), non-coding RNAs (ex: MicroRNAs) which results phenotypic modifications by individual genome reprograming. Otherwise, results from paternal exercise are inconclusive at this time.

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5

Taylor, Bethany C., and Nicolas L. Young. "Combinations of histone post-translational modifications." Biochemical Journal 478, no. 3 (February 10, 2021): 511–32. http://dx.doi.org/10.1042/bcj20200170.

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Histones are essential proteins that package the eukaryotic genome into its physiological state of nucleosomes, chromatin, and chromosomes. Post-translational modifications (PTMs) of histones are crucial to both the dynamic and persistent regulation of the genome. Histone PTMs store and convey complex signals about the state of the genome. This is often achieved by multiple variable PTM sites, occupied or unoccupied, on the same histone molecule or nucleosome functioning in concert. These mechanisms are supported by the structures of ‘readers’ that transduce the signal from the presence or absence of PTMs in specific cellular contexts. We provide background on PTMs and their complexes, review the known combinatorial function of PTMs, and assess the value and limitations of common approaches to measure combinatorial PTMs. This review serves as both a reference and a path forward to investigate combinatorial PTM functions, discover new synergies, and gather additional evidence supporting that combinations of histone PTMs are the central currency of chromatin-mediated regulation of the genome.

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6

Hattori, Takamitsu, Joseph M. Taft, Kalina M. Swist, Hao Luo, Heather Witt, Matthew Slattery, Akiko Koide, et al. "Recombinant antibodies to histone post-translational modifications." Nature Methods 10, no. 10 (August 18, 2013): 992–95. http://dx.doi.org/10.1038/nmeth.2605.

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7

Fan, Jing, Kimberly A. Krautkramer, Jessica L. Feldman, and John M. Denu. "Metabolic Regulation of Histone Post-Translational Modifications." ACS Chemical Biology 10, no. 1 (January 6, 2015): 95–108. http://dx.doi.org/10.1021/cb500846u.

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8

Tolsma, Thomas O., and Jeffrey C. Hansen. "Post-translational modifications and chromatin dynamics." Essays in Biochemistry 63, no. 1 (March 22, 2019): 89–96. http://dx.doi.org/10.1042/ebc20180067.

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Abstract The dynamic structure of chromatin is linked to gene regulation and many other biological functions. Consequently, it is of importance to understand the factors that regulate chromatin dynamics. While the in vivo analysis of chromatin has verified that histone post-translational modifications play a role in modulating DNA accessibility, the complex nuclear environment and multiplicity of modifications prevents clear conclusions as to how individual modifications influence chromatin dynamics in the cell. For this reason, in vitro analyses of model reconstituted nucleosomal arrays has been pivotal in understanding the dynamic nature of chromatin compaction and the affects that specific post-translational modifications can have on the higher order chromatin structure. In this mini-review, we briefly describe the dynamic chromatin structures that have been observed in vitro and the environmental conditions that give rise to these various conformational states. Our focus then turns to a discussion of the specific histone post-translational modifications that have been shown to alter formation of these higher order chromatin structures in vitro and how this may relate to the biological state and accessibility of chromatin in vivo.

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Méndez-Acuña, L., M. V. Di Tomaso, F. Palitti, and W. Martínez-López. "Histone Post-Translational Modifications in DNA Damage Response." Cytogenetic and Genome Research 128, no. 1-3 (2010): 28–36. http://dx.doi.org/10.1159/000296275.

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10

da Cunha, Julia Pinheiro Chagas, Ernesto Satoshi Nakayasu, Igor Correia de Almeida, and Sergio Schenkman. "Post-translational modifications of Trypanosoma cruzi histone H4." Molecular and Biochemical Parasitology 150, no. 2 (December 2006): 268–77. http://dx.doi.org/10.1016/j.molbiopara.2006.08.012.

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Sevilla, Ana, and Olivier Binda. "Post-translational modifications of the histone variant h2az." Stem Cell Research 12, no. 1 (January 2014): 289–95. http://dx.doi.org/10.1016/j.scr.2013.11.004.

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12

Minshull, Thomas C., and Mark J. Dickman. "Mass spectrometry analysis of histone post translational modifications." Drug Discovery Today: Disease Models 12 (2014): 41–48. http://dx.doi.org/10.1016/j.ddmod.2015.03.002.

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13

Andrés, Marta, Daniel García-Gomis, Inma Ponte, Pedro Suau, and Alicia Roque. "Histone H1 Post-Translational Modifications: Update and Future Perspectives." International Journal of Molecular Sciences 21, no. 16 (August 18, 2020): 5941. http://dx.doi.org/10.3390/ijms21165941.

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Histone H1 is the most variable histone and its role at the epigenetic level is less characterized than that of core histones. In vertebrates, H1 is a multigene family, which can encode up to 11 subtypes. The H1 subtype composition is different among cell types during the cell cycle and differentiation. Mass spectrometry-based proteomics has added a new layer of complexity with the identification of a large number of post-translational modifications (PTMs) in H1. In this review, we summarize histone H1 PTMs from lower eukaryotes to humans, with a particular focus on mammalian PTMs. Special emphasis is made on PTMs, whose molecular function has been described. Post-translational modifications in H1 have been associated with the regulation of chromatin structure during the cell cycle as well as transcriptional activation, DNA damage response, and cellular differentiation. Additionally, PTMs in histone H1 that have been linked to diseases such as cancer, autoimmune disorders, and viral infection are examined. Future perspectives and challenges in the profiling of histone H1 PTMs are also discussed.

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Hamam and Palaniyar. "Post-Translational Modifications in NETosis and NETs-Mediated Diseases." Biomolecules 9, no. 8 (August 14, 2019): 369. http://dx.doi.org/10.3390/biom9080369.

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: Neutrophils undergo a unique form of cell death that generates neutrophil extracellular traps (NETs) that may help to neutralize invading pathogens and restore homeostasis. However, uncontrolled NET formation (NETosis) can result in numerous diseases that adversely affect health. Recent studies further elucidate the mechanistic details of the different forms of NETosis and their common end structure, as NETs were constantly found to contain DNA, modified histones and cytotoxic enzymes. In fact, emerging evidence reveal that the post translational modifications (PTMs) of histones in neutrophils have a critical role in regulating neutrophil death. Histone citrullination is shown to promote a rapid form of NET formation independent of NADPH oxidase (NOX), which relies on calcium influx. Interestingly, few studies suggest an association between histone citrullination and other types of PTMs to control cell survival and death, such as histone methylation. Even more exciting is the finding that histone acetylation has a biphasic effect upon NETosis, where histone deacetylase (HDAC) inhibitors promote baseline, NOX-dependent and -independent NETosis. However, increasing levels of histone acetylation suppresses NETosis, and to switch neutrophil death to apoptosis. Interestingly, in the presence of NETosis-promoting stimuli, high levels of HDACis limit both NETosis and apoptosis, and promote neutrophil survival. Recent studies also reveal the importance of the PTMs of neutrophils in influencing numerous pathologies. Histone modifications in NETs can act as a double-edged sword, as they are capable of altering multiple types of neutrophil death, and influencing numerous NET-mediated diseases, such as acute lung injury (ALI), thrombosis, sepsis, systemic lupus erythematosus, and cancer progression. A clear understanding of the role of different PTMs in neutrophils would be important for an understanding of the molecular mechanisms of NETosis, and to appropriately treat NETs-mediated diseases.

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15

Liu, Yanli, and Jinrong Min. "Structure and function of histone methylation-binding proteins in plants." Biochemical Journal 473, no. 12 (June 10, 2016): 1663–80. http://dx.doi.org/10.1042/bcj20160123.

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Post-translational modifications of histones play important roles in modulating many essential biological processes in both animals and plants. These covalent modifications, including methylation, acetylation, phosphorylation, ubiquitination, SUMOylation and so on, are laid out and erased by histone-modifying enzymes and read out by effector proteins. Recent studies have revealed that a number of developmental processes in plants are under the control of histone post-translational modifications, such as floral transition, seed germination, organogenesis and morphogenesis. Therefore, it is critical to identify those protein domains, which could specifically recognize these post-translational modifications to modulate chromatin structure and regulate gene expression. In the present review, we discuss the recent progress in understanding the structure and function of the histone methylation readers in plants, by focusing on Arabidopsis thaliana proteins.

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Zhiteneva, Alisa, Juan Jose Bonfiglio, Alexandr Makarov, Thomas Colby, Paola Vagnarelli, Eric C. Schirmer, Ivan Matic, and William C. Earnshaw. "Mitotic post-translational modifications of histones promote chromatin compaction in vitro." Open Biology 7, no. 9 (September 2017): 170076. http://dx.doi.org/10.1098/rsob.170076.

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How eukaryotic chromosomes are compacted during mitosis has been a leading question in cell biology since the nineteenth century. Non-histone proteins such as condensin complexes contribute to chromosome shaping, but appear not to be necessary for mitotic chromatin compaction. Histone modifications are known to affect chromatin structure. As histones undergo major changes in their post-translational modifications during mitotic entry, we speculated that the spectrum of cell-cycle-specific histone modifications might contribute to chromosome compaction during mitosis. To test this hypothesis, we isolated core histones from interphase and mitotic cells and reconstituted chromatin with them. We used mass spectrometry to show that key post-translational modifications remained intact during our isolation procedure. Light, atomic force and transmission electron microscopy analysis showed that chromatin assembled from mitotic histones has a much greater tendency to aggregate than chromatin assembled from interphase histones, even under low magnesium conditions where interphase chromatin remains as separate beads-on-a-string structures. These observations are consistent with the hypothesis that mitotic chromosome formation is a two-stage process with changes in the spectrum of histone post-translational modifications driving mitotic chromatin compaction, while the action of non-histone proteins such as condensin may then shape the condensed chromosomes into their classic mitotic morphology.

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Chatterjee, Snehajyoti, Parijat Senapati, and Tapas K. Kundu. "Post-translational modifications of lysine in DNA-damage repair." Essays in Biochemistry 52 (May 25, 2012): 93–111. http://dx.doi.org/10.1042/bse0520093.

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DNA damage in cells is often the result of constant genotoxic insult. Nevertheless, efficient DNA repair pathways are able to maintain genomic integrity. Over the past decade it has been revealed that it is not only kinase signalling pathways which play a central role in this process, but also the different post-translational modifications at lysine residues of histone (chromatin) and non-histone proteins. These lysine modifications include acetylation, methylation, ubiquitination and SUMOylation. Genomic instability is often the major cause of different diseases, especially cancer, where lysine modifications are altered and thereby have an impact on the various DNA repair mechanisms. This chapter will discuss the recent advances in our understanding of the role of different lysine modifications in DNA repair and its physiological consequences.

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18

García-Giménez, José-Luis, Concepción Garcés, Carlos Romá-Mateo, and Federico V. Pallardó. "Oxidative stress-mediated alterations in histone post-translational modifications." Free Radical Biology and Medicine 170 (July 2021): 6–18. http://dx.doi.org/10.1016/j.freeradbiomed.2021.02.027.

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19

Monti, Barbara. "Histone Post-translational Modifications to Target Memory-related Diseases." Current Pharmaceutical Design 19, no. 28 (July 1, 2013): 5065–75. http://dx.doi.org/10.2174/1381612811319280005.

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20

Tian, Zhixin, Nikola Tolić, Rui Zhao, Ronald J. Moore, Shawna M. Hengel, Errol W. Robinson, David L. Stenoien, Si Wu, Richard D. Smith, and Ljiljana Paša-Tolić. "Enhanced top-down characterization of histone post-translational modifications." Genome Biology 13, no. 10 (2012): R86. http://dx.doi.org/10.1186/gb-2012-13-10-r86.

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21

Füllgrabe, Jens, Daniel J. Klionsky, and Bertrand Joseph. "Histone post-translational modifications regulate autophagy flux and outcome." Autophagy 9, no. 10 (October 25, 2013): 1621–23. http://dx.doi.org/10.4161/auto.25803.

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Bronner, Christian, Guy Fuhrmann, Frédéric L. Chédin, Marcella Macaluso, and Sirano Dhe-Paganon. "UHRF1 Links the Histone Code and DNA Methylation to Ensure Faithful Epigenetic Memory Inheritance." Genetics & Epigenetics 2 (January 2009): GEG.S3992. http://dx.doi.org/10.4137/geg.s3992.

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Epigenetics is the study of the transmission of cell memory through mitosis or meiosis that is not based on the DNA sequence. At the molecular level the epigenetic memory of a cell is embedded in DNA methylation, histone post-translational modifications, RNA interference and histone isoform variation. There is a tight link between histone post-translational modifications (the histone code) and DNA methylation, as modifications of histones contribute to the establishment of DNA methylation patterns and vice versa. Interestingly, proteins have recently been identified that can simultaneously read both methylated DNA and the histone code. UHRF1 fulfills these requirements by having unique structural domains that allow concurrent recognition of histone modifications and methylated DNA. Herein, we review our current knowledge of UHRF1 and discuss how this protein ensures the link between histone marks and DNA methylation. Understanding the molecular functions of this protein may reveal the physiological relevance of the linkage between these layers of epigenetic marks.

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23

Wang, Xiaodong, and Jeffrey J. Hayes. "Physical methods used to study core histone tail structures and interactions in solutionThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 4 (August 2006): 578–88. http://dx.doi.org/10.1139/o06-076.

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The core histone tail domains are key regulatory elements in chromatin. The tails are essential for folding oligonucleosomal arrays into both secondary and tertiary structures, and post-translational modifications within these domains can directly alter DNA accessibility. Unfortunately, there is little understanding of the structures and interactions of the core histone tail domains or how post-translational modifications within the tails may alter these interactions. Here we review NMR, thermal denaturation, cross-linking, and other selected solution methods used to define the general structures and binding behavior of the tail domains in various chromatin environments. All of these methods indicate that the tail domains bind primarily electrostatically to sites within chromatin. The data also indicate that the tails adopt specific structures when bound to DNA and that tail structures and interactions are plastic, depending on the specific chromatin environment. In addition, post-translational modifications, such as acetylation, can directly alter histone tail structures and interactions.

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24

Ito, K. "Impact of post-translational modifications of proteins on the inflammatory process." Biochemical Society Transactions 35, no. 2 (March 20, 2007): 281–83. http://dx.doi.org/10.1042/bst0350281.

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PTM (post-translational modification) is the chemical modification of a protein after its translation. The well-studied PTM is phosphorylation, but, recently, PTMs have been re-focused by extensive studies on histone modifications and the discovery of the ubiquitin system. Histone acetylation is the well-established epigenetic regulator for gene expression. Recent studies show that different patterns of PTMs and cross-talk of individual modifications (acetylation, methylation, phosphorylation) are keys of gene regulation (known as the ‘histone code’). As well as histone, non-histone proteins are also targets of acetylation. For instance, NF-κB (nuclear factor κB), a transcriptional factor, is regulated dynamically by acetylation/deacetylation. Acetylation of NF-κB [RelA (p65)] at Lys310 enhances its transcriptional activity, which is inhibited by SIRT1 deacetylase, type III HDAC (histone deacetylase). We also found that acetylated NF-κB preferentially bound to the IL-8 (interleukin 8) gene promoter, but not to GM-CSF (granulocyte/macrophage colony-stimulating factor), suggesting NF-κB acetylation is involved in selective gene induction as well as an increased level of transcription. A receptor of glucocorticoid, a potent anti-inflammatory agent, is also a target of acetylation. The glucocorticoid receptor is highly acetylated after ligand binding but its deacetylation is necessary for gene repression through binding to NF-κB. As well as acetylation, other PTMs, such as nitration, carbonylation and ubiquitination on transcriptional/nuclear factors, are taking part in the inflammatory process. Cross-talk of individual modifications on proteins deserves further evaluation in the future (as ‘protein code’).

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Nothof, Sophie A., Frédérique Magdinier, and Julien Van-Gils. "Chromatin Structure and Dynamics: Focus on Neuronal Differentiation and Pathological Implication." Genes 13, no. 4 (April 2, 2022): 639. http://dx.doi.org/10.3390/genes13040639.

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Chromatin structure is an essential regulator of gene expression. Its state of compaction contributes to the regulation of genetic programs, in particular during differentiation. Epigenetic processes, which include post-translational modifications of histones, DNA methylation and implication of non-coding RNA, are powerful regulators of gene expression. Neurogenesis and neuronal differentiation are spatio-temporally regulated events that allow the formation of the central nervous system components. Here, we review the chromatin structure and post-translational histone modifications associated with neuronal differentiation. Studying the impact of histone modifications on neuronal differentiation improves our understanding of the pathophysiological mechanisms of chromatinopathies and opens up new therapeutic avenues. In addition, we will discuss techniques for the analysis of histone modifications on a genome-wide scale and the pathologies associated with the dysregulation of the epigenetic machinery.

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Sales-Gil, Raquel, and Paola Vagnarelli. "How HP1 Post-Translational Modifications Regulate Heterochromatin Formation and Maintenance." Cells 9, no. 6 (June 12, 2020): 1460. http://dx.doi.org/10.3390/cells9061460.

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Heterochromatin Protein 1 (HP1) is a highly conserved protein that has been used as a classic marker for heterochromatin. HP1 binds to di- and tri-methylated histone H3K9 and regulates heterochromatin formation, functions and structure. Besides the well-established phosphorylation of histone H3 Ser10 that has been shown to modulate HP1 binding to chromatin, several studies have recently highlighted the importance of HP1 post-translational modifications and additional epigenetic features for the modulation of HP1-chromatin binding ability and heterochromatin formation. In this review, we summarize the recent literature of HP1 post-translational modifications that have contributed to understand how heterochromatin is formed, regulated and maintained.

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Garcia, Benjamin A. "Mass Spectrometric Analysis of Histone Variants and Post-translational Modifications." Frontiers in Bioscience S1, no. 1 (2009): 142–53. http://dx.doi.org/10.2741/s14.

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Starkova, T. Yu, A. M. Polyanichko, T. O. Artamonova, M. A. Khodorkovskii, E. I. Kostyleva, E. V. Chikhirzhina, and A. N. Tomilin. "Post-translational modifications of linker histone H1 variants in mammals." Physical Biology 14, no. 1 (February 16, 2017): 016005. http://dx.doi.org/10.1088/1478-3975/aa551a.

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Fukagawa, Tatsuo. "Critical histone post-translational modifications for centromere function and propagation." Cell Cycle 16, no. 13 (June 15, 2017): 1259–65. http://dx.doi.org/10.1080/15384101.2017.1325044.

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Chatterjee, A., N. Von Neuhoff, B. Skawran, L. Lauterboeck, N. Hofmann, and B. Glasmacher. "Cryopreservation alters the histone post-translational modifications of stem cells." Cryobiology 73, no. 3 (December 2016): 402. http://dx.doi.org/10.1016/j.cryobiol.2016.09.018.

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Perri, Angela Mena, Valter Agosti, Erika Olivo, Antonio Concolino, MariaTeresa De Angelis, Laura Tammè, Claudia Vincenza Fiumara, Giovanni Cuda, and Domenica Scumaci. "Histone proteomics reveals novel post-translational modifications in breast cancer." Aging 11, no. 23 (December 8, 2019): 11722–55. http://dx.doi.org/10.18632/aging.102577.

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Cobos, Samantha N., Seth A. Bennett, and Mariana P. Torrente. "The impact of histone post-translational modifications in neurodegenerative diseases." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1865, no. 8 (August 2019): 1982–91. http://dx.doi.org/10.1016/j.bbadis.2018.10.019.

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Galligan, James, James Wepy, Matthew Streeter, Philip Kingsley, Michelle Mitchener, Orrette Wauchope, William Beavers, et al. "Methylglyoxal-derived post-translational arginine modifications are abundant histone marks." Free Radical Biology and Medicine 128 (November 2018): S137. http://dx.doi.org/10.1016/j.freeradbiomed.2018.10.362.

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Draker, Ryan, and Peter Cheung. "Transcriptional and epigenetic functions of histone variant H2A.ZThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB’s 51st Annual Meeting – Epigenetics and Chromatin Dynamics, and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 87, no. 1 (February 2009): 19–25. http://dx.doi.org/10.1139/o08-117.

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The chromatin organization of a genome ultimately dictates the gene expression profile of the cell. It is now well recognized that key mechanisms that regulate chromatin structure include post-translational modifications of histones and the incorporation of histone variants at strategic sites within the genome. H2A.Z is a variant of H2A that is localized to the 5′ end of many genes and is required for proper regulation of gene expression. However, its precise function in the transcription process is not yet well defined. In this review, we discuss some of the recent findings related to this histone variant, how it associates with other histone epigenetic marks, and how post-translational modifications of H2A.Z further define its function.

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McManus, Kirk J., and Michael J. Hendzel. "The relationship between histone H3 phosphorylation and acetylation throughout the mammalian cell cycleThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 4 (August 2006): 640–57. http://dx.doi.org/10.1139/o06-086.

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During interphase, histone amino-terminal tails play important roles in regulating the extent of DNA compaction. Post-translational modifications of the histone tails are intimately associated with regulating chromatin structure: phosphorylation of histone H3 is associated with proper chromosome condensation and dynamics during mitosis, while multiple H2B, H3, and H4 tail acetylations destabilize the chromatin fiber and are sufficient to decondense chromatin fibers in vitro. In this study, we investigate the spatio-temporal dynamics of specific histone H3 phosphorylations and acetylations to better understand the interplay of these post-translational modifications throughout the cell cycle. Using a panel of antibodies that individually, or in combination, recognize phosphorylated serines 10 and 28 and acetylated lysines 9 and 14, we define a series of changes associated with histone H3 that occur as cells progress through the cell cycle. Our results establish that mitosis appears to be a period of the cell cycle when many modifications are highly dynamic. Furthermore, they suggest that the upstream histone acetyltransferases/deacetylases and kinase/phosphatases are temporally regulated to alter their function globally during specific cell cycle time points.

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Corujo, David, and Marcus Buschbeck. "Post-Translational Modifications of H2A Histone Variants and Their Role in Cancer." Cancers 10, no. 3 (February 27, 2018): 59. http://dx.doi.org/10.3390/cancers10030059.

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Histone variants are chromatin components that replace replication-coupled histones in a fraction of nucleosomes and confer particular characteristics to chromatin. H2A variants represent the most numerous and diverse group among histone protein families. In the nucleosomal structure, H2A-H2B dimers can be removed and exchanged more easily than the stable H3-H4 core. The unstructured N-terminal histone tails of all histones, but also the C-terminal tails of H2A histones protrude out of the compact structure of the nucleosome core. These accessible tails are the preferential target sites for a large number of post-translational modifications (PTMs). While some PTMs are shared between replication-coupled H2A and H2A variants, many modifications are limited to a specific histone variant. The present review focuses on the H2A variants H2A.Z, H2A.X, and macroH2A, and summarizes their functions in chromatin and how these are linked to cancer development and progression. H2A.Z primarily acts as an oncogene and macroH2A and H2A.X as tumour suppressors. We further focus on the regulation by PTMs, which helps to understand a degree of context dependency.

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Drury, Georgina E., Adam A. Dowle, David A. Ashford, Wanda M. Waterworth, Jerry Thomas, and Christopher E. West. "Dynamics of plant histone modifications in response to DNA damage." Biochemical Journal 445, no. 3 (July 13, 2012): 393–401. http://dx.doi.org/10.1042/bj20111956.

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DNA damage detection and repair take place in the context of chromatin, and histone proteins play important roles in these events. Post-translational modifications of histone proteins are involved in repair and DNA damage signalling processes in response to genotoxic stresses. In particular, acetylation of histones H3 and H4 plays an important role in the mammalian and yeast DNA damage response and survival under genotoxic stress. However, the role of post-translational modifications to histones during the plant DNA damage response is currently poorly understood. Several different acetylated H3 and H4 N-terminal peptides following X-ray treatment were identified using MS analysis of purified histones, revealing previously unseen patterns of histone acetylation in Arabidopsis. Immunoblot analysis revealed an increase in the relative abundance of the H3 acetylated N-terminus, and a global decrease in hyperacetylation of H4 in response to DNA damage induced by X-rays. Conversely, mutants in the key DNA damage signalling factor ATM (ATAXIA TELANGIECTASIA MUTATED) display increased histone acetylation upon irradiation, linking the DNA damage response with dynamic changes in histone modification in plants.

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Simon, Marek, Sarah Javaid, Alex Mooney, Mridula Manohar, Richard Fishel, Jennifer J. Ottesen, and Michael G. Poirier. "Histone Post-Translational Modifications Buried within the Nucleosome DNA-Histone Interface Facilitate Nucleosome Disassembly." Biophysical Journal 98, no. 3 (January 2010): 477a. http://dx.doi.org/10.1016/j.bpj.2009.12.2599.

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Guttzeit, Sebastian, and Johannes Backs. "Post-translational modifications talk and crosstalk to class IIa histone deacetylases." Journal of Molecular and Cellular Cardiology 162 (January 2022): 53–61. http://dx.doi.org/10.1016/j.yjmcc.2021.08.007.

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Bergmüller, Eveline, Peter M. Gehrig, and Wilhelm Gruissem. "Characterization of Post-Translational Modifications of Histone H2B-Variants Isolated fromArabidopsisthaliana." Journal of Proteome Research 6, no. 9 (September 2007): 3655–68. http://dx.doi.org/10.1021/pr0702159.

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Makalowska, I., E. S. Ferlanti, A. D. Baxevanis, and D. Landsman. "Histone Sequence Database: sequences, structures, post-translational modifications and genetic loci." Nucleic Acids Research 27, no. 1 (January 1, 1999): 323–24. http://dx.doi.org/10.1093/nar/27.1.323.

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KNAPP, A., C. REN, X. SU, D. LUCAS, J. BYRD, M. FREITAS, and M. PARTHUN. "Quantitative profiling of histone post-translational modifications by stable isotope labeling." Methods 41, no. 3 (March 2007): 312–19. http://dx.doi.org/10.1016/j.ymeth.2006.08.017.

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Buuh, Zakey Yusuf, Zhigang Lyu, and Rongsheng E. Wang. "Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins." Journal of Medicinal Chemistry 61, no. 8 (May 15, 2017): 3239–52. http://dx.doi.org/10.1021/acs.jmedchem.6b01817.

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Cruickshank, Mark N., Paul Besant, and Daniela Ulgiati. "The impact of histone post-translational modifications on developmental gene regulation." Amino Acids 39, no. 5 (March 5, 2010): 1087–105. http://dx.doi.org/10.1007/s00726-010-0530-6.

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Franzoni, Alessandra, Nadia Passon, Dora Fabbro, Mario Tiribelli, Daniela Damiani, and Giuseppe Damante. "Histone post-translational modifications associated to BAALC expression in leukemic cells." Biochemical and Biophysical Research Communications 417, no. 2 (January 2012): 721–25. http://dx.doi.org/10.1016/j.bbrc.2011.12.013.

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Taverna, Sean D., C. David Allis, and Sandra B. Hake. "“Hunt”-ing for post-translational modifications that underlie the histone code." International Journal of Mass Spectrometry 259, no. 1-3 (January 2007): 40–45. http://dx.doi.org/10.1016/j.ijms.2006.07.009.

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Tessier, Shannon N., Bryan E. Luu, Jeffrey C. Smith, and Kenneth B. Storey. "The role of global histone post-translational modifications during mammalian hibernation." Cryobiology 75 (April 2017): 28–36. http://dx.doi.org/10.1016/j.cryobiol.2017.02.008.

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Redon, Christophe E., Urbain Weyemi, Palak R. Parekh, Dejun Huang, Allison S. Burrell, and William M. Bonner. "γ-H2AX and other histone post-translational modifications in the clinic." Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 1819, no. 7 (July 2012): 743–56. http://dx.doi.org/10.1016/j.bbagrm.2012.02.021.

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Zhang, Liwen, Ericka E. Eugeni, Mark R. Parthun, and Michael A. Freitas. "Identification of novel histone post-translational modifications by peptide mass fingerprinting." Chromosoma 112, no. 2 (August 1, 2003): 77–86. http://dx.doi.org/10.1007/s00412-003-0244-6.

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Esteves de Lima, Joana, and Frédéric Relaix. "Epigenetic Regulation of Myogenesis: Focus on the Histone Variants." International Journal of Molecular Sciences 22, no. 23 (November 25, 2021): 12727. http://dx.doi.org/10.3390/ijms222312727.

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Skeletal muscle development and regeneration rely on the successive activation of specific transcription factors that engage cellular fate, promote commitment, and drive differentiation. Emerging evidence demonstrates that epigenetic regulation of gene expression is crucial for the maintenance of the cell differentiation status upon division and, therefore, to preserve a specific cellular identity. This depends in part on the regulation of chromatin structure and its level of condensation. Chromatin architecture undergoes remodeling through changes in nucleosome composition, such as alterations in histone post-translational modifications or exchange in the type of histone variants. The mechanisms that link histone post-translational modifications and transcriptional regulation have been extensively evaluated in the context of cell fate and differentiation, whereas histone variants have attracted less attention in the field. In this review, we discuss the studies that have provided insights into the role of histone variants in the regulation of myogenic gene expression, myoblast differentiation, and maintenance of muscle cell identity.

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