User:Cassandra Marsh/Sandbox 1
From Proteopedia
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[https://en.wikipedia.org/wiki/Histone Histones] are a family of basic, positively charged proteins that associate with DNA inside the nucleus to help condense the DNA into [https://en.wikipedia.org/wiki/Chromatin chromatin] <ref name="Histones"> Histones | Learn Science at Scitable https://www.nature.com/scitable/definition/histone-histones-57</ref>. The nuclear DNA is wrapped around the histone in order to fit in the nucleus. [https://en.wikipedia.org/wiki/Nucleosome Nucleosomes] are chromatin beads made up of DNA wrapped around eight histone proteins, or a [https://en.wikipedia.org/wiki/Histone_octamer histone octamer] <ref name="Histones" />. Four different examples of modifying histones including [https://en.wikipedia.org/wiki/Histone_acetylation_and_deacetylation Histone acetylation, Histone deacetylation], [https://en.wikipedia.org/wiki/Histone_methylation Histone methylation] and [https://en.wikipedia.org/wiki/Demethylase Histone demethylation] <ref name="Histones" />. | [https://en.wikipedia.org/wiki/Histone Histones] are a family of basic, positively charged proteins that associate with DNA inside the nucleus to help condense the DNA into [https://en.wikipedia.org/wiki/Chromatin chromatin] <ref name="Histones"> Histones | Learn Science at Scitable https://www.nature.com/scitable/definition/histone-histones-57</ref>. The nuclear DNA is wrapped around the histone in order to fit in the nucleus. [https://en.wikipedia.org/wiki/Nucleosome Nucleosomes] are chromatin beads made up of DNA wrapped around eight histone proteins, or a [https://en.wikipedia.org/wiki/Histone_octamer histone octamer] <ref name="Histones" />. Four different examples of modifying histones including [https://en.wikipedia.org/wiki/Histone_acetylation_and_deacetylation Histone acetylation, Histone deacetylation], [https://en.wikipedia.org/wiki/Histone_methylation Histone methylation] and [https://en.wikipedia.org/wiki/Demethylase Histone demethylation] <ref name="Histones" />. | ||
| + | ===Histone Deacetylases (HDACs)=== | ||
| + | ε-Amino-lysine acetylation is a type of modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni" />. There are different classes of HDACs based on phylogenetic analysis: | ||
| - | ===HDAC8=== | + | •Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3 |
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| + | •Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1 <ref name="Vanninni">doi: :10.1038/sj.embor.7401047</ref>. | ||
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| + | HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. | ||
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| + | ====HDAC8==== | ||
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is | [https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is | ||
Revision as of 18:42, 5 April 2019
Histone Deacetylase 8 (HDAC 8), H. sapians
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References
- ↑ 1.0 1.1 1.2 Histones | Learn Science at Scitable https://www.nature.com/scitable/definition/histone-histones-57
- ↑ 2.0 2.1 2.2 . PMID:216315890657
Student Contributors
- Cassandra Marsh
- Courtney Brown
- Carolyn Hurdle
