Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease
Linker histones (LH) are a critical component of chromatin in addition to the canonical histones (H2A, H2B, H3, and H4). In humans, 11 subtypes (7 somatic and 4 germinal) of linker histones have been identified, and their diverse cellular functions in chromatin structure, DNA replication, DNA repair...
Gespeichert in:
| Veröffentlicht in: | International journal of molecular sciences 2023-01, Vol.24 (2), p.1463 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 2 |
| container_start_page | 1463 |
| container_title | International journal of molecular sciences |
| container_volume | 24 |
| creator | Kumar, Ashok Maurya, Preeti Hayes, Jeffrey J |
| description | Linker histones (LH) are a critical component of chromatin in addition to the canonical histones (H2A, H2B, H3, and H4). In humans, 11 subtypes (7 somatic and 4 germinal) of linker histones have been identified, and their diverse cellular functions in chromatin structure, DNA replication, DNA repair, transcription, and apoptosis have been explored, especially for the somatic subtypes. Delineating the unique role of human linker histone (hLH) and their subtypes is highly tedious given their high homology and overlapping expression patterns. However, recent advancements in mass spectrometry combined with HPLC have helped in identifying the post-translational modifications (PTMs) found on the different LH subtypes. However, while a number of PTMs have been identified and their potential nuclear and non-nuclear functions explored in cellular processes, there are very few studies delineating the direct relevance of these PTMs in diseases. In addition, recent whole-genome sequencing of clinical samples from cancer patients and individuals afflicted with Rahman syndrome have identified high-frequency mutations and therefore broadened the perspective of the linker histone mutations in diseases. In this review, we compile the identified PTMs of hLH subtypes, current knowledge of the relevance of hLH PTMs in human diseases, and the correlation of PTMs coinciding with mutations mapped in diseases. |
| doi_str_mv | 10.3390/ijms24021463 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9860689</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2768232713</sourcerecordid><originalsourceid>FETCH-LOGICAL-c412t-8f7781e4b18adc3d740ffc1b8a873f5b346635af5820dff9588479541b4e7a6b3</originalsourceid><addsrcrecordid>eNpdkc2P0zAUxC0Eot3CjTOyxIXDBvwV2-GAhJaFIrUCiXK2nMSmLond9UuQ-t-TbsuqcLJH7-fRGw9CLyh5w3lF3oZdD0wQRoXkj9CcCsYKQqR6fHGfoSuAHSGMs7J6imZcSiUqTeeo_5ZgKDbZRujsEFLE69QGH5p7AdjGFq_H4aySx8uxtxGvQvzlMl4GGFJ0-PtYD4e9g3d4s3Uh47WNwTs4PcMh4o8BnAX3DD3xtgP3_Hwu0I9Pt5ubZbH6-vnLzYdV0QjKhkJ7pTR1oqbatg1vlSDeN7TWVivuy5oLKXlpfakZab2vSq2FqkpBa-GUlTVfoPcn3_1Y965tXByy7cw-h97mg0k2mH8nMWzNz_TbVFoSqavJ4PXZIKe7cUpi-gCN6zobXRrBMCX19JmK8gl99R-6S2OOU7wjpRjTFVUTdX2impwAsvMPy1Bijj2ayx4n_OVlgAf4b3H8DwRjmto</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2767228917</pqid></control><display><type>article</type><title>Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease</title><source>MDPI - Multidisciplinary Digital Publishing Institute</source><source>MEDLINE</source><source>Free E-Journal (出版社公開部分のみ）</source><source>PubMed Central</source><creator>Kumar, Ashok ; Maurya, Preeti ; Hayes, Jeffrey J</creator><creatorcontrib>Kumar, Ashok ; Maurya, Preeti ; Hayes, Jeffrey J</creatorcontrib><description>Linker histones (LH) are a critical component of chromatin in addition to the canonical histones (H2A, H2B, H3, and H4). In humans, 11 subtypes (7 somatic and 4 germinal) of linker histones have been identified, and their diverse cellular functions in chromatin structure, DNA replication, DNA repair, transcription, and apoptosis have been explored, especially for the somatic subtypes. Delineating the unique role of human linker histone (hLH) and their subtypes is highly tedious given their high homology and overlapping expression patterns. However, recent advancements in mass spectrometry combined with HPLC have helped in identifying the post-translational modifications (PTMs) found on the different LH subtypes. However, while a number of PTMs have been identified and their potential nuclear and non-nuclear functions explored in cellular processes, there are very few studies delineating the direct relevance of these PTMs in diseases. In addition, recent whole-genome sequencing of clinical samples from cancer patients and individuals afflicted with Rahman syndrome have identified high-frequency mutations and therefore broadened the perspective of the linker histone mutations in diseases. In this review, we compile the identified PTMs of hLH subtypes, current knowledge of the relevance of hLH PTMs in human diseases, and the correlation of PTMs coinciding with mutations mapped in diseases.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms24021463</identifier><identifier>PMID: 36674981</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino acids ; Apoptosis ; Cell cycle ; Cellular structure ; Chromatin ; Chromatography ; Critical components ; Cyclin-dependent kinases ; Deoxyribonucleic acid ; DNA ; DNA biosynthesis ; DNA methylation ; DNA repair ; DNA structure ; Epigenetics ; Genomes ; Histones ; Histones - metabolism ; Homology ; Humans ; Identification ; Insects ; Kinases ; Mammals ; Mass Spectrometry ; Mass spectroscopy ; Mutation ; Peptides ; Phosphorylation ; Post-translation ; Protein Processing, Post-Translational - genetics ; Proteins ; Review ; Scientific imaging ; Whole genome sequencing</subject><ispartof>International journal of molecular sciences, 2023-01, Vol.24 (2), p.1463</ispartof><rights>2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2023 by the authors. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-8f7781e4b18adc3d740ffc1b8a873f5b346635af5820dff9588479541b4e7a6b3</citedby><cites>FETCH-LOGICAL-c412t-8f7781e4b18adc3d740ffc1b8a873f5b346635af5820dff9588479541b4e7a6b3</cites><orcidid>0000-0001-6482-0137</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9860689/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9860689/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36674981$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kumar, Ashok</creatorcontrib><creatorcontrib>Maurya, Preeti</creatorcontrib><creatorcontrib>Hayes, Jeffrey J</creatorcontrib><title>Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Linker histones (LH) are a critical component of chromatin in addition to the canonical histones (H2A, H2B, H3, and H4). In humans, 11 subtypes (7 somatic and 4 germinal) of linker histones have been identified, and their diverse cellular functions in chromatin structure, DNA replication, DNA repair, transcription, and apoptosis have been explored, especially for the somatic subtypes. Delineating the unique role of human linker histone (hLH) and their subtypes is highly tedious given their high homology and overlapping expression patterns. However, recent advancements in mass spectrometry combined with HPLC have helped in identifying the post-translational modifications (PTMs) found on the different LH subtypes. However, while a number of PTMs have been identified and their potential nuclear and non-nuclear functions explored in cellular processes, there are very few studies delineating the direct relevance of these PTMs in diseases. In addition, recent whole-genome sequencing of clinical samples from cancer patients and individuals afflicted with Rahman syndrome have identified high-frequency mutations and therefore broadened the perspective of the linker histone mutations in diseases. In this review, we compile the identified PTMs of hLH subtypes, current knowledge of the relevance of hLH PTMs in human diseases, and the correlation of PTMs coinciding with mutations mapped in diseases.</description><subject>Amino acids</subject><subject>Apoptosis</subject><subject>Cell cycle</subject><subject>Cellular structure</subject><subject>Chromatin</subject><subject>Chromatography</subject><subject>Critical components</subject><subject>Cyclin-dependent kinases</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA biosynthesis</subject><subject>DNA methylation</subject><subject>DNA repair</subject><subject>DNA structure</subject><subject>Epigenetics</subject><subject>Genomes</subject><subject>Histones</subject><subject>Histones - metabolism</subject><subject>Homology</subject><subject>Humans</subject><subject>Identification</subject><subject>Insects</subject><subject>Kinases</subject><subject>Mammals</subject><subject>Mass Spectrometry</subject><subject>Mass spectroscopy</subject><subject>Mutation</subject><subject>Peptides</subject><subject>Phosphorylation</subject><subject>Post-translation</subject><subject>Protein Processing, Post-Translational - genetics</subject><subject>Proteins</subject><subject>Review</subject><subject>Scientific imaging</subject><subject>Whole genome sequencing</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkc2P0zAUxC0Eot3CjTOyxIXDBvwV2-GAhJaFIrUCiXK2nMSmLond9UuQ-t-TbsuqcLJH7-fRGw9CLyh5w3lF3oZdD0wQRoXkj9CcCsYKQqR6fHGfoSuAHSGMs7J6imZcSiUqTeeo_5ZgKDbZRujsEFLE69QGH5p7AdjGFq_H4aySx8uxtxGvQvzlMl4GGFJ0-PtYD4e9g3d4s3Uh47WNwTs4PcMh4o8BnAX3DD3xtgP3_Hwu0I9Pt5ubZbH6-vnLzYdV0QjKhkJ7pTR1oqbatg1vlSDeN7TWVivuy5oLKXlpfakZab2vSq2FqkpBa-GUlTVfoPcn3_1Y965tXByy7cw-h97mg0k2mH8nMWzNz_TbVFoSqavJ4PXZIKe7cUpi-gCN6zobXRrBMCX19JmK8gl99R-6S2OOU7wjpRjTFVUTdX2impwAsvMPy1Bijj2ayx4n_OVlgAf4b3H8DwRjmto</recordid><startdate>20230111</startdate><enddate>20230111</enddate><creator>Kumar, Ashok</creator><creator>Maurya, Preeti</creator><creator>Hayes, Jeffrey J</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-6482-0137</orcidid></search><sort><creationdate>20230111</creationdate><title>Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease</title><author>Kumar, Ashok ; Maurya, Preeti ; Hayes, Jeffrey J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-8f7781e4b18adc3d740ffc1b8a873f5b346635af5820dff9588479541b4e7a6b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Amino acids</topic><topic>Apoptosis</topic><topic>Cell cycle</topic><topic>Cellular structure</topic><topic>Chromatin</topic><topic>Chromatography</topic><topic>Critical components</topic><topic>Cyclin-dependent kinases</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA biosynthesis</topic><topic>DNA methylation</topic><topic>DNA repair</topic><topic>DNA structure</topic><topic>Epigenetics</topic><topic>Genomes</topic><topic>Histones</topic><topic>Histones - metabolism</topic><topic>Homology</topic><topic>Humans</topic><topic>Identification</topic><topic>Insects</topic><topic>Kinases</topic><topic>Mammals</topic><topic>Mass Spectrometry</topic><topic>Mass spectroscopy</topic><topic>Mutation</topic><topic>Peptides</topic><topic>Phosphorylation</topic><topic>Post-translation</topic><topic>Protein Processing, Post-Translational - genetics</topic><topic>Proteins</topic><topic>Review</topic><topic>Scientific imaging</topic><topic>Whole genome sequencing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kumar, Ashok</creatorcontrib><creatorcontrib>Maurya, Preeti</creatorcontrib><creatorcontrib>Hayes, Jeffrey J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest research library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content (ProQuest)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kumar, Ashok</au><au>Maurya, Preeti</au><au>Hayes, Jeffrey J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2023-01-11</date><risdate>2023</risdate><volume>24</volume><issue>2</issue><spage>1463</spage><pages>1463-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Linker histones (LH) are a critical component of chromatin in addition to the canonical histones (H2A, H2B, H3, and H4). In humans, 11 subtypes (7 somatic and 4 germinal) of linker histones have been identified, and their diverse cellular functions in chromatin structure, DNA replication, DNA repair, transcription, and apoptosis have been explored, especially for the somatic subtypes. Delineating the unique role of human linker histone (hLH) and their subtypes is highly tedious given their high homology and overlapping expression patterns. However, recent advancements in mass spectrometry combined with HPLC have helped in identifying the post-translational modifications (PTMs) found on the different LH subtypes. However, while a number of PTMs have been identified and their potential nuclear and non-nuclear functions explored in cellular processes, there are very few studies delineating the direct relevance of these PTMs in diseases. In addition, recent whole-genome sequencing of clinical samples from cancer patients and individuals afflicted with Rahman syndrome have identified high-frequency mutations and therefore broadened the perspective of the linker histone mutations in diseases. In this review, we compile the identified PTMs of hLH subtypes, current knowledge of the relevance of hLH PTMs in human diseases, and the correlation of PTMs coinciding with mutations mapped in diseases.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>36674981</pmid><doi>10.3390/ijms24021463</doi><orcidid>https://orcid.org/0000-0001-6482-0137</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1422-0067 |
| ispartof | International journal of molecular sciences, 2023-01, Vol.24 (2), p.1463 |
| issn | 1422-0067 1661-6596 1422-0067 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9860689 |
| source | MDPI - Multidisciplinary Digital Publishing Institute; MEDLINE; Free E-Journal (出版社公開部分のみ）; PubMed Central |
| subjects | Amino acids Apoptosis Cell cycle Cellular structure Chromatin Chromatography Critical components Cyclin-dependent kinases Deoxyribonucleic acid DNA DNA biosynthesis DNA methylation DNA repair DNA structure Epigenetics Genomes Histones Histones - metabolism Homology Humans Identification Insects Kinases Mammals Mass Spectrometry Mass spectroscopy Mutation Peptides Phosphorylation Post-translation Protein Processing, Post-Translational - genetics Proteins Review Scientific imaging Whole genome sequencing |
| title | Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-04T15%3A09%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Post-Translation%20Modifications%20and%20Mutations%20of%20Human%20Linker%20Histone%20Subtypes:%20Their%20Manifestation%20in%20Disease&rft.jtitle=International%20journal%20of%20molecular%20sciences&rft.au=Kumar,%20Ashok&rft.date=2023-01-11&rft.volume=24&rft.issue=2&rft.spage=1463&rft.pages=1463-&rft.issn=1422-0067&rft.eissn=1422-0067&rft_id=info:doi/10.3390/ijms24021463&rft_dat=%3Cproquest_pubme%3E2768232713%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2767228917&rft_id=info:pmid/36674981&rfr_iscdi=true |