User:Asif Hossain/Sandbox 1: Difference between revisions

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== Introduction ==

Histone deacetylase 8 (HDAC8) is an enzyme that plays a role in controlling gene expression. Specifically, HDAC8 removes an acetyl group off of the ε-amino-Lys 382 of Histone 4's N-terminal core.<ref name="Vannini, A., Volpari, C., Gallinari, P.">Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., ... & Di Marco, S. (2007). Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex. EMBO reports, 8(9), 879-884. https://doi.org/10.1038/sj.embor.7401047 </ref> [https://en.wikipedia.org/wiki/Histone Histones] consist of eight monomers to form an octomer complex. Each histone has a positive charge which allows interaction with negatively-charged DNA. This prevents transcription factors from accessing DNA, thus, decreasing gene expression. [https://en.wikipedia.org/wiki/Chromatin_remodeling Chromatin remodeling] by histone ~~acetylation and/or deacetylation~~ is ~~an example~~ of [https://en.wikipedia.org/wiki/Epigenetics epigenetic regulation]. [https://en.wikipedia.org/wiki/Histone_acetyltransferase Histone Acetylase 1] (HAT1) catalyzes the addition of an acetyl group onto a histone. The lack of charge on the acetyl group weakens the interaction between DNA and histones which allows transcription factors to access the DNA to increase gene expression. HDAC8 reverses this reaction by catalyzing the removal of these acetyl groups from the Lys to reclaim the positive charge of the histone. This allows the histone to interact with the negative charge on the DNA. As a result, DNA binds more tightly to the histone protein, repressing transcription and gene expression.

Histone deacetylase 8 (HDAC8) is an enzyme that plays a role in controlling gene expression. Specifically, HDAC8 removes an acetyl group off of the ε-amino-Lys 382 of Histone 4's N-terminal core.<ref name="Vannini, A., Volpari, C., Gallinari, P.">Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., ... & Di Marco, S. (2007). Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex. EMBO reports, 8(9), 879-884. https://doi.org/10.1038/sj.embor.7401047 </ref> [https://en.wikipedia.org/wiki/Histone Histones] consist of eight monomers to form an octomer complex. Each histone has a positive charge which allows interaction with negatively-charged DNA. This prevents transcription factors from accessing DNA, thus, decreasing gene expression. [https://en.wikipedia.org/wiki/Chromatin_remodeling Chromatin remodeling] by the addition or removal of an acetyl group off a histone is a form of [https://en.wikipedia.org/wiki/Epigenetics epigenetic regulation]. [https://en.wikipedia.org/wiki/Histone_acetyltransferase Histone Acetylase 1] (HAT1) catalyzes the addition of an acetyl group onto a histone. The lack of charge on the acetyl group weakens the interaction between DNA and histones which allows transcription factors to access the DNA to increase gene expression. HDAC8 reverses this reaction by catalyzing the removal of these acetyl groups from the Lys to reclaim the positive charge of the histone. This allows the histone to interact with the negative charge on the DNA. As a result, DNA binds more tightly to the histone protein, repressing transcription and gene expression.

==HDAC Enzymes and Homology==

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 == Introduction ==
-Histone deacetylase 8 (HDAC8) is an enzyme that plays a role in controlling gene expression. Specifically, HDAC8 removes an acetyl group off of the ε-amino-Lys 382 of Histone 4's N-terminal core.<ref name="Vannini, A., Volpari, C., Gallinari, P.">Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., ... & Di Marco, S. (2007). Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex. EMBO reports, 8(9), 879-884. https://doi.org/10.1038/sj.embor.7401047 </ref> [https://en.wikipedia.org/wiki/Histone Histones] consist of eight monomers to form an octomer complex. Each histone has a positive charge which allows interaction with negatively-charged DNA. This prevents transcription factors from accessing DNA, thus, decreasing gene expression. [https://en.wikipedia.org/wiki/Chromatin_remodeling Chromatin remodeling] by histone acetylation and/or deacetylation is an example of [https://en.wikipedia.org/wiki/Epigenetics epigenetic regulation]. [https://en.wikipedia.org/wiki/Histone_acetyltransferase Histone Acetylase 1] (HAT1) catalyzes the addition of an acetyl group onto a histone. The lack of charge on the acetyl group weakens the interaction between DNA and histones which allows transcription factors to access the DNA to increase gene expression. HDAC8 reverses this reaction by catalyzing the removal of these acetyl groups from the Lys to reclaim the positive charge of the histone. This allows the histone to interact with the negative charge on the DNA. As a result, DNA binds more tightly to the histone protein, repressing transcription and gene expression.
+Histone deacetylase 8 (HDAC8) is an enzyme that plays a role in controlling gene expression. Specifically, HDAC8 removes an acetyl group off of the ε-amino-Lys 382 of Histone 4's N-terminal core.<ref name="Vannini, A., Volpari, C., Gallinari, P.">Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., ... & Di Marco, S. (2007). Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex. EMBO reports, 8(9), 879-884. https://doi.org/10.1038/sj.embor.7401047 </ref> [https://en.wikipedia.org/wiki/Histone Histones] consist of eight monomers to form an octomer complex. Each histone has a positive charge which allows interaction with negatively-charged DNA. This prevents transcription factors from accessing DNA, thus, decreasing gene expression. [https://en.wikipedia.org/wiki/Chromatin_remodeling Chromatin remodeling] by the addition or removal of an acetyl group off a histone is a form of [https://en.wikipedia.org/wiki/Epigenetics epigenetic regulation]. [https://en.wikipedia.org/wiki/Histone_acetyltransferase Histone Acetylase 1] (HAT1) catalyzes the addition of an acetyl group onto a histone. The lack of charge on the acetyl group weakens the interaction between DNA and histones which allows transcription factors to access the DNA to increase gene expression. HDAC8 reverses this reaction by catalyzing the removal of these acetyl groups from the Lys to reclaim the positive charge of the histone. This allows the histone to interact with the negative charge on the DNA. As a result, DNA binds more tightly to the histone protein, repressing transcription and gene expression.
 ==HDAC Enzymes and Homology==