Sandbox Reserved 1546: Difference between revisions
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==Relevance== | ==Relevance== | ||
=Purpose of the Study= | |||
It is known that the 5h86 Human Gcn5 enzyme functions as an acetyltransferase that regulates transcription by acetylating the N-terminal tails of histones <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. The experiment was tested on Gcn5 (Gcn5L2), more specifically the lysine acetylation of this enzyme <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. This is important to understand because the acyltransferase activity of the Gcn5L2 becomes much weaker with increasing acyl chain length <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. The researchers were inspired by previous studies that identified a chemically diverse array of lysine acyl modification in vivo, and more specifically - the acyl chain of acetyltransferase specificity in the human Gcn5 <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. In short, they want to experiment and test which acyl-chain donor had the highest enzymatic activity and to characterize the specificity of the acyl-chain of the human Gcn5, which catalyzes the acetylation of histone peptides much quicker than other methods like propionylation or butyrylation <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. Through the experiment, it was found that via this method, the active sites of Gcn5 can accommodate longer acyl chains without many structural rearrangements <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. | It is known that the 5h86 Human Gcn5 enzyme functions as an acetyltransferase that regulates transcription by acetylating the N-terminal tails of histones <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. The experiment was tested on Gcn5 (Gcn5L2), more specifically the lysine acetylation of this enzyme <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. This is important to understand because the acyltransferase activity of the Gcn5L2 becomes much weaker with increasing acyl chain length <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. The researchers were inspired by previous studies that identified a chemically diverse array of lysine acyl modification in vivo, and more specifically - the acyl chain of acetyltransferase specificity in the human Gcn5 <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. In short, they want to experiment and test which acyl-chain donor had the highest enzymatic activity and to characterize the specificity of the acyl-chain of the human Gcn5, which catalyzes the acetylation of histone peptides much quicker than other methods like propionylation or butyrylation <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. Through the experiment, it was found that via this method, the active sites of Gcn5 can accommodate longer acyl chains without many structural rearrangements <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. | ||
=Experimental Procedure= | |||
<p>This experiment was completed in various parts:</p> | <p>This experiment was completed in various parts:</p> | ||
<p>1. '''Protein Expression and Purification'''</p> | <p>1. '''Protein Expression and Purification'''</p> | ||
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<p>5. '''PDB Accession Codes'''</p> | <p>5. '''PDB Accession Codes'''</p> | ||
<p>• This step composed of data entry into the Protein Data Bank (PDB)</p> | <p>• This step composed of data entry into the Protein Data Bank (PDB)</p> | ||
=Experimental Results= | |||
=Future Steps= | |||
== References == | == References == | ||
<references/> | <references/> | ||
