User:Cassandra Marsh/Sandbox 1
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===Histone Deacetylases (HDACs)=== | ===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: | + | ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">doi:10.1038/sj.embor.7401047</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis: |
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3 | •Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3 | ||
| - | •Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1 <ref name="Vanninni" | + | •Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1 |
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| + | •Class III - Sirtuin deacetylases | ||
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| + | •Class IV - HDAC 11 <ref name="Vanninni" />. | ||
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. | HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. | ||
Current revision
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 doi: https://dx.doi.org/10.1038/sj.embor.7401047
Student Contributors
- Cassandra Marsh
- Courtney Brown
- Carolyn Hurdle
