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Quickly evolving histones, nucleosome stability and chromatin folding: All about histone H2A.Bbd
Histone H2A.Bbd ( Barr body- deficient) is a novel histone variant which is largely excluded from the inactive X chromosome of mammals. Discovered only 6 years ago, H2A.Bbd displays very unusual structural and functional properties, for instance, it is relatively shorter and only 48% identical compa...
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Published in: | Gene 2008-04, Vol.413 (1), p.1-7 |
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description | Histone H2A.Bbd (
Barr
body-
deficient) is a novel histone variant which is largely excluded from the inactive X chromosome of mammals. Discovered only 6 years ago, H2A.Bbd displays very unusual structural and functional properties, for instance, it is relatively shorter and only 48% identical compared to H2A, lacking both the typical C-terminal tail of the H2A family and the very last sequence of the docking domain, making it the most specialized among all histone variants known to date. Indeed, molecular evolutionary analyses have shown that H2A.Bbd is a highly hypervariable and quickly evolving protein exclusive to mammalian lineages, in striking contrast to all other histones. Different studies have described a deposition pattern of H2A.Bbd in the chromatin that overlaps with regions of histone H4 acetylation suggesting its association with transcriptionally active euchromatic regions of the genome. In this regard, it is believed that this histone variant plays an important role in determining such regions by destabilizing the nucleosome and locally unfolding the chromatin fiber. This review provides a concise, comprehensive and timely summary of the work published on H2A.Bbd structure and function. Special emphasis is placed on its chromatin deposition patterns in relation to gene expression profiles and its evolutionary history, as well as on the dynamics of H2A.Bbd-containing nucleosomes. |
doi_str_mv | 10.1016/j.gene.2008.02.003 |
format | article |
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Barr
body-
deficient) is a novel histone variant which is largely excluded from the inactive X chromosome of mammals. Discovered only 6 years ago, H2A.Bbd displays very unusual structural and functional properties, for instance, it is relatively shorter and only 48% identical compared to H2A, lacking both the typical C-terminal tail of the H2A family and the very last sequence of the docking domain, making it the most specialized among all histone variants known to date. Indeed, molecular evolutionary analyses have shown that H2A.Bbd is a highly hypervariable and quickly evolving protein exclusive to mammalian lineages, in striking contrast to all other histones. Different studies have described a deposition pattern of H2A.Bbd in the chromatin that overlaps with regions of histone H4 acetylation suggesting its association with transcriptionally active euchromatic regions of the genome. In this regard, it is believed that this histone variant plays an important role in determining such regions by destabilizing the nucleosome and locally unfolding the chromatin fiber. This review provides a concise, comprehensive and timely summary of the work published on H2A.Bbd structure and function. Special emphasis is placed on its chromatin deposition patterns in relation to gene expression profiles and its evolutionary history, as well as on the dynamics of H2A.Bbd-containing nucleosomes.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/j.gene.2008.02.003</identifier><identifier>PMID: 18329190</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Binding Sites ; Chromatin Assembly and Disassembly - genetics ; Chromatin Assembly and Disassembly - physiology ; Chromosomal Instability ; Chromosomes ; Evolution ; Evolution, Molecular ; Gene Expression ; Genetic Variation ; Histone variants ; Histones - chemistry ; Histones - genetics ; Histones - physiology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Nucleosomes ; Nucleosomes - genetics ; Nucleosomes - physiology ; Phylogeny ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid</subject><ispartof>Gene, 2008-04, Vol.413 (1), p.1-7</ispartof><rights>2008 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-a5ab8d727926dda5d884463bf18f8f55fb6930ab1a553a8a9a7b64920a54bc893</citedby><cites>FETCH-LOGICAL-c451t-a5ab8d727926dda5d884463bf18f8f55fb6930ab1a553a8a9a7b64920a54bc893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18329190$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>González-Romero, Rodrigo</creatorcontrib><creatorcontrib>Méndez, Josefina</creatorcontrib><creatorcontrib>Ausió, Juan</creatorcontrib><creatorcontrib>Eirín-López, José M.</creatorcontrib><title>Quickly evolving histones, nucleosome stability and chromatin folding: All about histone H2A.Bbd</title><title>Gene</title><addtitle>Gene</addtitle><description>Histone H2A.Bbd (
Barr
body-
deficient) is a novel histone variant which is largely excluded from the inactive X chromosome of mammals. Discovered only 6 years ago, H2A.Bbd displays very unusual structural and functional properties, for instance, it is relatively shorter and only 48% identical compared to H2A, lacking both the typical C-terminal tail of the H2A family and the very last sequence of the docking domain, making it the most specialized among all histone variants known to date. Indeed, molecular evolutionary analyses have shown that H2A.Bbd is a highly hypervariable and quickly evolving protein exclusive to mammalian lineages, in striking contrast to all other histones. Different studies have described a deposition pattern of H2A.Bbd in the chromatin that overlaps with regions of histone H4 acetylation suggesting its association with transcriptionally active euchromatic regions of the genome. In this regard, it is believed that this histone variant plays an important role in determining such regions by destabilizing the nucleosome and locally unfolding the chromatin fiber. This review provides a concise, comprehensive and timely summary of the work published on H2A.Bbd structure and function. Special emphasis is placed on its chromatin deposition patterns in relation to gene expression profiles and its evolutionary history, as well as on the dynamics of H2A.Bbd-containing nucleosomes.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Chromatin Assembly and Disassembly - genetics</subject><subject>Chromatin Assembly and Disassembly - physiology</subject><subject>Chromosomal Instability</subject><subject>Chromosomes</subject><subject>Evolution</subject><subject>Evolution, Molecular</subject><subject>Gene Expression</subject><subject>Genetic Variation</subject><subject>Histone variants</subject><subject>Histones - chemistry</subject><subject>Histones - genetics</subject><subject>Histones - physiology</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nucleosomes</subject><subject>Nucleosomes - genetics</subject><subject>Nucleosomes - physiology</subject><subject>Phylogeny</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Homology, Amino Acid</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNqFkU1v1DAURS0EaofSP8ACecWqCc9OnNgVm2kFFKkSQqJr1x8vrQcnLnEy0vz7ZjSDugNvnhfn3MW9hLxnUDJgzadN-YADlhxAlsBLgOoVWTHZqmL5ytdkBVUrC8aYOiVvc97A8oTgJ-SUyYorpmBF7n_Owf2OO4rbFLdheKCPIU9pwHxBh9lFTDn1SPNkbIhh2lEzeOoex9SbKQy0S9Ev0iVdx0iNTfP016c3fF1eWf-OvOlMzHh-vGfk7uuXX9c3xe2Pb9-v17eFqwWbCiOMlb7lreKN90Z4Keu6qWzHZCc7ITrbqAqMZUaIykijTGubWnEworZOquqMfDzkPo3pz4x50n3IDmM0A6Y56xbqthYg_wty4LytFCwgP4BuTDmP2OmnMfRm3GkGej-A3uj9AHo_gAaul9YX6cMxfbY9-hfl2PgCfD4AuJSxDTjq7AIODn0Y0U3ap_Cv_GeVG5cG</recordid><startdate>20080430</startdate><enddate>20080430</enddate><creator>González-Romero, Rodrigo</creator><creator>Méndez, Josefina</creator><creator>Ausió, Juan</creator><creator>Eirín-López, José M.</creator><general>Elsevier B.V</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20080430</creationdate><title>Quickly evolving histones, nucleosome stability and chromatin folding: All about histone H2A.Bbd</title><author>González-Romero, Rodrigo ; Méndez, Josefina ; Ausió, Juan ; Eirín-López, José M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-a5ab8d727926dda5d884463bf18f8f55fb6930ab1a553a8a9a7b64920a54bc893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Chromatin Assembly and Disassembly - genetics</topic><topic>Chromatin Assembly and Disassembly - physiology</topic><topic>Chromosomal Instability</topic><topic>Chromosomes</topic><topic>Evolution</topic><topic>Evolution, Molecular</topic><topic>Gene Expression</topic><topic>Genetic Variation</topic><topic>Histone variants</topic><topic>Histones - chemistry</topic><topic>Histones - genetics</topic><topic>Histones - physiology</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nucleosomes</topic><topic>Nucleosomes - genetics</topic><topic>Nucleosomes - physiology</topic><topic>Phylogeny</topic><topic>Protein Structure, Tertiary</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>González-Romero, Rodrigo</creatorcontrib><creatorcontrib>Méndez, Josefina</creatorcontrib><creatorcontrib>Ausió, Juan</creatorcontrib><creatorcontrib>Eirín-López, José M.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Gene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>González-Romero, Rodrigo</au><au>Méndez, Josefina</au><au>Ausió, Juan</au><au>Eirín-López, José M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quickly evolving histones, nucleosome stability and chromatin folding: All about histone H2A.Bbd</atitle><jtitle>Gene</jtitle><addtitle>Gene</addtitle><date>2008-04-30</date><risdate>2008</risdate><volume>413</volume><issue>1</issue><spage>1</spage><epage>7</epage><pages>1-7</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><abstract>Histone H2A.Bbd (
Barr
body-
deficient) is a novel histone variant which is largely excluded from the inactive X chromosome of mammals. Discovered only 6 years ago, H2A.Bbd displays very unusual structural and functional properties, for instance, it is relatively shorter and only 48% identical compared to H2A, lacking both the typical C-terminal tail of the H2A family and the very last sequence of the docking domain, making it the most specialized among all histone variants known to date. Indeed, molecular evolutionary analyses have shown that H2A.Bbd is a highly hypervariable and quickly evolving protein exclusive to mammalian lineages, in striking contrast to all other histones. Different studies have described a deposition pattern of H2A.Bbd in the chromatin that overlaps with regions of histone H4 acetylation suggesting its association with transcriptionally active euchromatic regions of the genome. In this regard, it is believed that this histone variant plays an important role in determining such regions by destabilizing the nucleosome and locally unfolding the chromatin fiber. This review provides a concise, comprehensive and timely summary of the work published on H2A.Bbd structure and function. Special emphasis is placed on its chromatin deposition patterns in relation to gene expression profiles and its evolutionary history, as well as on the dynamics of H2A.Bbd-containing nucleosomes.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>18329190</pmid><doi>10.1016/j.gene.2008.02.003</doi><tpages>7</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Binding Sites Chromatin Assembly and Disassembly - genetics Chromatin Assembly and Disassembly - physiology Chromosomal Instability Chromosomes Evolution Evolution, Molecular Gene Expression Genetic Variation Histone variants Histones - chemistry Histones - genetics Histones - physiology Humans Models, Molecular Molecular Sequence Data Nucleosomes Nucleosomes - genetics Nucleosomes - physiology Phylogeny Protein Structure, Tertiary Sequence Homology, Amino Acid |
title | Quickly evolving histones, nucleosome stability and chromatin folding: All about histone H2A.Bbd |
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