Short Histone H2A Variants: Small in Stature but not in Function
The dynamic packaging of DNA into chromatin regulates all aspects of genome function by altering the accessibility of DNA and by providing docking pads to proteins that copy, repair and express the genome. Different epigenetic-based mechanisms have been described that alter the way DNA is organised...
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| Format: | Article |
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MDPI AG
2020-04-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/9/4/867 |
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| author | Xuanzhao Jiang Tatiana A. Soboleva David J. Tremethick |
| author_facet | Xuanzhao Jiang Tatiana A. Soboleva David J. Tremethick |
| author_sort | Xuanzhao Jiang |
| collection | DOAJ |
| description | The dynamic packaging of DNA into chromatin regulates all aspects of genome function by altering the accessibility of DNA and by providing docking pads to proteins that copy, repair and express the genome. Different epigenetic-based mechanisms have been described that alter the way DNA is organised into chromatin, but one fundamental mechanism alters the biochemical composition of a nucleosome by substituting one or more of the core histones with their variant forms. Of the core histones, the largest number of histone variants belong to the H2A class. The most divergent class is the designated “short H2A variants” (H2A.B, H2A.L, H2A.P and H2A.Q), so termed because they lack a H2A C-terminal tail. These histone variants appeared late in evolution in eutherian mammals and are lineage-specific, being expressed in the testis (and, in the case of H2A.B, also in the brain). To date, most information about the function of these peculiar histone variants has come from studies on the H2A.B and H2A.L family in mice. In this review, we describe their unique protein characteristics, their impact on chromatin structure, and their known functions plus other possible, even non-chromatin, roles in an attempt to understand why these peculiar histone variants evolved in the first place. |
| first_indexed | 2024-03-10T20:42:33Z |
| format | Article |
| id | doaj.art-09e9afdcd4a541558a810ac246766a6d |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-10T20:42:33Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-09e9afdcd4a541558a810ac246766a6d2023-11-19T20:32:34ZengMDPI AGCells2073-44092020-04-019486710.3390/cells9040867Short Histone H2A Variants: Small in Stature but not in FunctionXuanzhao Jiang0Tatiana A. Soboleva1David J. Tremethick2The John Curtin School of Medical Research, The Australian National University, P.O. Box 334, 2601 Canberra, AustraliaThe John Curtin School of Medical Research, The Australian National University, P.O. Box 334, 2601 Canberra, AustraliaThe John Curtin School of Medical Research, The Australian National University, P.O. Box 334, 2601 Canberra, AustraliaThe dynamic packaging of DNA into chromatin regulates all aspects of genome function by altering the accessibility of DNA and by providing docking pads to proteins that copy, repair and express the genome. Different epigenetic-based mechanisms have been described that alter the way DNA is organised into chromatin, but one fundamental mechanism alters the biochemical composition of a nucleosome by substituting one or more of the core histones with their variant forms. Of the core histones, the largest number of histone variants belong to the H2A class. The most divergent class is the designated “short H2A variants” (H2A.B, H2A.L, H2A.P and H2A.Q), so termed because they lack a H2A C-terminal tail. These histone variants appeared late in evolution in eutherian mammals and are lineage-specific, being expressed in the testis (and, in the case of H2A.B, also in the brain). To date, most information about the function of these peculiar histone variants has come from studies on the H2A.B and H2A.L family in mice. In this review, we describe their unique protein characteristics, their impact on chromatin structure, and their known functions plus other possible, even non-chromatin, roles in an attempt to understand why these peculiar histone variants evolved in the first place.https://www.mdpi.com/2073-4409/9/4/867chromatinnucleosomeshistone variantsH2A.BH2A.Lacidic patch |
| spellingShingle | Xuanzhao Jiang Tatiana A. Soboleva David J. Tremethick Short Histone H2A Variants: Small in Stature but not in Function Cells chromatin nucleosomes histone variants H2A.B H2A.L acidic patch |
| title | Short Histone H2A Variants: Small in Stature but not in Function |
| title_full | Short Histone H2A Variants: Small in Stature but not in Function |
| title_fullStr | Short Histone H2A Variants: Small in Stature but not in Function |
| title_full_unstemmed | Short Histone H2A Variants: Small in Stature but not in Function |
| title_short | Short Histone H2A Variants: Small in Stature but not in Function |
| title_sort | short histone h2a variants small in stature but not in function |
| topic | chromatin nucleosomes histone variants H2A.B H2A.L acidic patch |
| url | https://www.mdpi.com/2073-4409/9/4/867 |
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