Histone H3: Difference between revisions
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{{Short description|One of the five main histone proteins}} |
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{{infobox protein |
{{infobox protein |
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| Name = H3 histone, family 3A (H3.3A) |
| Name = H3 histone, family 3A (H3.3A) |
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[[File:Basic units of chromatin structure.svg|thumb|Basic units of chromatin structure]] |
[[File:Basic units of chromatin structure.svg|thumb|Basic units of chromatin structure]] |
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'''Histone H3''' is one of the five main [[histone]]s involved in the structure of [[chromatin]] in [[eukaryotic cell]]s.<ref name="Bhasin_2006">{{cite journal | vauthors = Bhasin M, Reinherz EL, Reche PA | title = Recognition and classification of histones using support vector machine | journal = Journal of Computational Biology | volume = 13 | issue = 1 | pages = 102–12 | year = 2006 | pmid = 16472024 | doi = 10.1089/cmb.2006.13.102 | url = https://eprints.ucm.es/9328/1/31.Reche_etal_MI_2006.pdf }}</ref><ref name="HartlFreilfelder&Snyder">{{ |
'''Histone H3''' is one of the five main [[histone]]s involved in the structure of [[chromatin]] in [[eukaryotic cell]]s.<ref name="Bhasin_2006">{{cite journal | vauthors = Bhasin M, Reinherz EL, Reche PA | title = Recognition and classification of histones using support vector machine | journal = Journal of Computational Biology | volume = 13 | issue = 1 | pages = 102–12 | year = 2006 | pmid = 16472024 | doi = 10.1089/cmb.2006.13.102 | url = https://eprints.ucm.es/9328/1/31.Reche_etal_MI_2006.pdf }}</ref><ref name="HartlFreilfelder&Snyder">{{cite book | last1 = Hartl | first1 = Daniel L. | last2 = Freifelder | first2 = David | last3 = Snyder | first3 = Leon A. | name-list-style = vanc |year=1988 |title=Basic Genetics |location=Boston |publisher=Jones and Bartlett Publishers |isbn=978-0-86720-090-4 |url-access=registration |url=https://archive.org/details/basicgenetics0000hart }}</ref> Featuring a main globular domain and a long [[N-terminal end|N-terminal tail]], H3 is involved with the structure of the [[nucleosome]]s of the 'beads on a string' structure. Histone proteins are highly [[post-translationally modified]] however Histone H3 is the most extensively modified of the five histones. The term "Histone H3" alone is purposely ambiguous in that it does not distinguish between sequence variants or modification state. Histone H3 is an important protein in the emerging field of [[epigenetics]], where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes. |
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== Epigenetics and post-translational modifications == |
== Epigenetics and post-translational modifications == |
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| ⚫ | The [[N-terminus]] of H3 protrudes from the globular [[nucleosome]] core and is susceptible to post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to [[lysine]] and [[arginine]] amino acids and the phosphorylation of [[serine]] or [[threonine]]. Di- and Tri-methylation of lysine 9 are associated with repression and [[heterochromatin]] (see [[H3K9me2]] and [[H3K9me3]]), while mono-methylation of K4 (K4 corresponds to lysine residue at 4th position)(see [[H3K4me1]]), is associated with active genes.<ref name="Rosenfeld_2009">{{cite journal | vauthors = Rosenfeld JA, Wang Z, Schones DE, Zhao K, DeSalle R, Zhang MQ | title = Determination of enriched histone modifications in non-genic portions of the human genome | journal = BMC Genomics | volume = 10 | pages = 143 | date = March 2009 | pmid = 19335899 | pmc = 2667539 | doi = 10.1186/1471-2164-10-143 | doi-access = free }}</ref><ref name="pmid11242053">{{cite journal |vauthors=Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T |date=Mar 2001 |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins |url=https://www.nature.com/articles/35065132 |journal=Nature |volume=410 |issue=6824 |pages=116–20 |bibcode=2001Natur.410..116L |doi=10.1038/35065132 |pmid=11242053 |s2cid=4331863}}</ref> Acetylation of histone H3 at several lysine positions in the histone tail is performed by [[histone acetyltransferase]] enzymes (HATs). Acetylation of lysine14 is commonly seen in genes that are being actively transcribed into [[RNA]] (see [[H3K14ac]]). |
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[[File:Basic units of chromatin structure.svg|thumb|Basic units of chromatin structure]] |
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| ⚫ | The N-terminus of H3 protrudes from the globular [[nucleosome]] core and is susceptible to post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to [[lysine]] and [[arginine]] amino acids and the phosphorylation of [[serine]] or [[threonine]]. Di- and Tri-methylation of lysine 9 are associated with repression and [[heterochromatin]] (see [[H3K9me2]] and [[H3K9me3]]), while mono-methylation of K4 (K4 corresponds to lysine residue at 4th position) is associated with active genes.<ref name="Rosenfeld_2009">{{cite journal | vauthors = Rosenfeld JA, Wang Z, Schones DE, Zhao K, DeSalle R, Zhang MQ | title = Determination of enriched histone modifications in non-genic portions of the human genome | journal = BMC Genomics | volume = 10 | pages = 143 | date = March 2009 | pmid = 19335899 | pmc = 2667539 | doi = 10.1186/1471-2164-10-143 }}</ref><ref name="pmid11242053">{{cite journal | |
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== Sequence variants == |
== Sequence variants == |
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Mammalian cells have seven known sequence variants of histone H3. These are denoted as Histone H3.1, Histone H3.2, Histone H3.3, Histone H3.4 (H3T), Histone H3.5, Histone H3.X and Histone H3.Y but have highly conserved sequences differing only by a few amino acids.<ref name="pmid12408966">{{cite journal | |
Mammalian cells have seven known sequence variants of histone H3. These are denoted as Histone H3.1, Histone H3.2, Histone H3.3, Histone H3.4 (H3T), Histone H3.5, Histone H3.X and Histone H3.Y but have highly conserved sequences differing only by a few amino acids.<ref name="pmid12408966">{{cite journal |vauthors=Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ |date=Nov 2002 |title=The human and mouse replication-dependent histone genes |url=https://www.sciencedirect.com/science/article/abs/pii/S0888754302968503 |journal=Genomics |volume=80 |issue=5 |pages=487–98 |doi=10.1016/S0888-7543(02)96850-3 |pmid=12408966}}</ref><ref name="pmid16267050">{{cite journal | vauthors = Hake SB, Garcia BA, Duncan EM, Kauer M, Dellaire G, Shabanowitz J, Bazett-Jones DP, Allis CD, Hunt DF | title = Expression patterns and post-translational modifications associated with mammalian histone H3 variants | journal = The Journal of Biological Chemistry | volume = 281 | issue = 1 | pages = 559–68 | date = Jan 2006 | pmid = 16267050 | doi = 10.1074/jbc.M509266200 | doi-access = free }}</ref> Histone H3.3 has been found to play an important role in maintaining genome integrity during mammalian development.<ref>{{cite journal | vauthors = Jang CW, Shibata Y, Starmer J, Yee D, Magnuson T | title = Histone H3.3 maintains genome integrity during mammalian development | journal = Genes & Development | volume = 29 | issue = 13 | pages = 1377–92 | date = Jul 2015 | pmid = 26159997 | doi = 10.1101/gad.264150.115 | pmc=4511213}}</ref> Histone variants from different organisms, their classification and variant specific features can be found in [https://www.ncbi.nlm.nih.gov/projects/HistoneDB2.0/index.fcgi/type/H3/ "HistoneDB - with Variants"] database. |
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== Genetics == |
== Genetics == |
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== See also == |
== See also == |
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* [[Histone code]] |
* [[Histone code#Histone H3]] |
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*Other [[histone]] [[proteins]]: |
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[[Histone H1|H1]] |
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[[Histone H2A|H2A]] |
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[[Histone H2B|H2B]] |
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[[Histone H4|H4]] |
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* [[Nucleosome]] |
* [[Nucleosome]] |
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* [[Histone]] |
* [[Histone]] |
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Latest revision as of 18:41, 22 April 2024
| H3 histone, family 3A (H3.3A) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | H3F3A | ||||||
| Alt. symbols | H3F3 | ||||||
| NCBI gene | 3020 | ||||||
| HGNC | 4764 | ||||||
| OMIM | 601128 | ||||||
| RefSeq | NM_002107 | ||||||
| UniProt | Q66I33 | ||||||
| Other data | |||||||
| Locus | Chr. 1 q41 | ||||||
| |||||||
| H3 histone, family 3B (H3.3B) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | H3F3B | ||||||
| NCBI gene | 3021 | ||||||
| HGNC | 4765 | ||||||
| OMIM | 601058 | ||||||
| RefSeq | NM_005324 | ||||||
| UniProt | P84243 | ||||||
| Other data | |||||||
| Locus | Chr. 17 q25 | ||||||
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Histone H3 is one of the five main histones involved in the structure of chromatin in eukaryotic cells.[1][2] Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. Histone proteins are highly post-translationally modified however Histone H3 is the most extensively modified of the five histones. The term "Histone H3" alone is purposely ambiguous in that it does not distinguish between sequence variants or modification state. Histone H3 is an important protein in the emerging field of epigenetics, where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes.
Epigenetics and post-translational modifications
[edit]The N-terminus of H3 protrudes from the globular nucleosome core and is susceptible to post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Di- and Tri-methylation of lysine 9 are associated with repression and heterochromatin (see H3K9me2 and H3K9me3), while mono-methylation of K4 (K4 corresponds to lysine residue at 4th position)(see H3K4me1), is associated with active genes.[3][4] Acetylation of histone H3 at several lysine positions in the histone tail is performed by histone acetyltransferase enzymes (HATs). Acetylation of lysine14 is commonly seen in genes that are being actively transcribed into RNA (see H3K14ac).
Sequence variants
[edit]Mammalian cells have seven known sequence variants of histone H3. These are denoted as Histone H3.1, Histone H3.2, Histone H3.3, Histone H3.4 (H3T), Histone H3.5, Histone H3.X and Histone H3.Y but have highly conserved sequences differing only by a few amino acids.[5][6] Histone H3.3 has been found to play an important role in maintaining genome integrity during mammalian development.[7] Histone variants from different organisms, their classification and variant specific features can be found in "HistoneDB - with Variants" database.
Genetics
[edit]Histone H3s are coded by several genes in the human genome, including:
- H3.1: HIST1H3A, HIST1H3B, HIST1H3C, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J
- H3.2: HIST2H3A, HIST2H3C, HIST2H3D
- H3.3: H3F3A, H3F3B
See also
[edit]References
[edit]- ^ Bhasin M, Reinherz EL, Reche PA (2006). "Recognition and classification of histones using support vector machine" (PDF). Journal of Computational Biology. 13 (1): 102–12. doi:10.1089/cmb.2006.13.102. PMID 16472024.
- ^ Hartl DL, Freifelder D, Snyder LA (1988). Basic Genetics. Boston: Jones and Bartlett Publishers. ISBN 978-0-86720-090-4.
- ^ Rosenfeld JA, Wang Z, Schones DE, Zhao K, DeSalle R, Zhang MQ (March 2009). "Determination of enriched histone modifications in non-genic portions of the human genome". BMC Genomics. 10: 143. doi:10.1186/1471-2164-10-143. PMC 2667539. PMID 19335899.
- ^ Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T (Mar 2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature. 410 (6824): 116–20. Bibcode:2001Natur.410..116L. doi:10.1038/35065132. PMID 11242053. S2CID 4331863.
- ^ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Nov 2002). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- ^ Hake SB, Garcia BA, Duncan EM, Kauer M, Dellaire G, Shabanowitz J, Bazett-Jones DP, Allis CD, Hunt DF (Jan 2006). "Expression patterns and post-translational modifications associated with mammalian histone H3 variants". The Journal of Biological Chemistry. 281 (1): 559–68. doi:10.1074/jbc.M509266200. PMID 16267050.
- ^ Jang CW, Shibata Y, Starmer J, Yee D, Magnuson T (Jul 2015). "Histone H3.3 maintains genome integrity during mammalian development". Genes & Development. 29 (13): 1377–92. doi:10.1101/gad.264150.115. PMC 4511213. PMID 26159997.