Keyword; Acetylation, Deacetylation

Acetylation / Deacetylation related products
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Acetylation of histones

Protein acetylation has been reported mainly in histones which regulate DNA binding. Histones are highly acetylated in active chromatin. In contrast, they stay under low acetylated state in inactive chromatin.

The residues with amino acid number are acetylation sites. The N-terminal regions of histones are rich of basic amino acids and lysine residues of them are acetylated.

Acetylation of p53

Recently, CBP and P/CAF which have the activities of histone acetyltransferase (HAT) have been reported to acetylate p53. p53 is a famous tumor suppressor pretein.

p53 is expressed in response to various types of stress involving DNA damage. It exerts antiproliferation effects for tumor suppression through the ability to function as a sequence-specific DNA-binding transcription factor.The acetylation of p53 stimulates its sequence-specific DNA-binding activity. This results in activation of p53 as a transcription factor.

Acetylation of lysine residues in C-terminal region results in neutralization of positive charges and leads to the disruption of interactions between the C-terminal domain and the core domain. DNA-binding domain adopts an active conformation and binds to target DNA.

Deacetylation of pRB

The retinoblastoma protein (Rb) is also a famous tumore suppressor protein. Rb binds to the activation domain of E2F and then actively represses the promoter by a mechanism that is poorly understood. It has been recently reported that Rb associates with a histone deacetylase, HDAC1, through the Rb 'pocket' domain. Rb cooperates with HDAC1 to repress the promoter of the gene related to cell-cycle. Active transcriptional repression by Rb may involve the modification of chromatin structure.

Phosphorylation / Dephosphorylation related products
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