Sandbox Reserved 1546: Difference between revisions

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<center>'''Figure 1''': Reaction mechanism of Acetoacetyl-CoA to two Acetyl-CoAs with the enzyme thiolase. Image obtained from class powerpoints.</center>

The specific acetyltransferase we are particularly interested in is known as 5H86 which is a Human Gcn5 bound to butyryl-CoA <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. Gcn5 is a conserved acetyltransferase that regulates transcription by acetylating the N-terminal tails of histones <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. To better understand how 5H86 is related to fatty acid degradation, we have to understand how they operate as a histone acetyltransferase (HATs). HATs are enzymes that acetylate conserved lysine amino acids on histone proteins <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. This occurs by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. When DNA is wrapped around histones, an acetyl group is transferred to the histones, allowing genes to be turned on and off <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. In conclusion, histone acetylation contribute to the increase of gene expression <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>.

hi

HATs also have a role in transcription regulation and are regulated through phosphorylation <ref name = "Regulating histone acetyltransferases and deacetylases">doi: 10.1038/sj.embor.embor941</ref>. For example, the HAT activity of the CREB-binding protein (CBP) is stimulated by the phosphorylation of a cyclin E/cyclin-dependent kinase 2 <ref name = "Regulating histone acetyltransferases and deacetylases"/>. HATs also participate in the genome-wide yield of acetyl groups on histones <ref name = "Regulating histone acetyltransferases and deacetylases"/>. Some HATs also target specific promoters through their physical interaction with sequence-specific transcription factors, sectionally modifying histones or transcription components to regulate gene transcription <ref name = "Regulating histone acetyltransferases and deacetylases"/>.

In all, the function of the 5H68 Human Gcn5 acetyltransferase can be represented through histone acetylation. Histone acetylation functions as the main switch that allows the interchange between permissive and repressive chromatin domains during transcription <ref name = "Role of histone acetylation in the control of gene expression">DOI: 10.1139/o05-041</ref>. The histone acetylation-dependent control of gene expression has mechanisms underlying a direct effect on the solidity of nucleosomal arrays and the creation of key sites for the regulatory binding proteins <ref name = "Role of histone acetylation in the control of gene expression"/>. The enzymes devoted to the addition and removal of acetyl groups are histone acetyltransferases, such as the 5H68 Human Gcn5 acetyltransferase, and deacetylases, in which both enzymes complete acetyl group removal or addition by removing the lysine residues on the N-terminals of histone tails <ref name = "Role of histone acetylation in the control of gene expression"/>.

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 <p><center>'''Figure 1''': Reaction mechanism of Acetoacetyl-CoA to two Acetyl-CoAs with the enzyme thiolase. Image obtained from class powerpoints.</center></p>
 <p>The specific acetyltransferase we are particularly interested in is known as 5H86 which is a Human Gcn5 bound to butyryl-CoA <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. Gcn5 is a conserved acetyltransferase that regulates transcription by acetylating the N-terminal tails of histones <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. To better understand how 5H86 is related to fatty acid degradation, we have to understand how they operate as a histone acetyltransferase (HATs). HATs are enzymes that acetylate conserved lysine amino acids on histone proteins <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. This occurs by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. When DNA is wrapped around histones, an acetyl group is transferred to the histones, allowing genes to be turned on and off <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. In conclusion, histone acetylation contribute to the increase of gene expression <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>.</p>
-<p>hi</p>
+<p>HATs also have a role in transcription regulation and are regulated through phosphorylation <ref name = "Regulating histone acetyltransferases and deacetylases">doi: 10.1038/sj.embor.embor941</ref>. For example, the HAT activity of the CREB-binding protein (CBP) is stimulated by the phosphorylation of a cyclin E/cyclin-dependent kinase 2 <ref name = "Regulating histone acetyltransferases and deacetylases"/>. HATs also participate in the genome-wide yield of acetyl groups on histones <ref name = "Regulating histone acetyltransferases and deacetylases"/>. Some HATs also target specific promoters through their physical interaction with sequence-specific transcription factors, sectionally modifying histones or transcription components to regulate gene transcription <ref name = "Regulating histone acetyltransferases and deacetylases"/>.</p>
+<p> In all, the function of the 5H68 Human Gcn5 acetyltransferase can be represented through histone acetylation. Histone acetylation functions as the main switch that allows the interchange between permissive and repressive chromatin domains during transcription <ref name = "Role of histone acetylation in the control of gene expression">DOI: 10.1139/o05-041</ref>. The histone acetylation-dependent control of gene expression has mechanisms underlying a direct effect on the solidity of nucleosomal arrays and the creation of key sites for the regulatory binding proteins <ref name = "Role of histone acetylation in the control of gene expression"/>. The enzymes devoted to the addition and removal of acetyl groups are histone acetyltransferases, such as the 5H68 Human Gcn5 acetyltransferase, and deacetylases, in which both enzymes complete acetyl group removal or addition by removing the lysine residues on the N-terminals of histone tails <ref name = "Role of histone acetylation in the control of gene expression"/>.</p>

Sandbox Reserved 1546: Difference between revisions

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