Date of Submission
Importance of Acetylation in p53
This is a critical review of an article titled “Acetylation of p53 Activates Transcription through Recruitment of Coactivators/Histone Acetyltransferases” (Barlev, Nickolai, Chehab, Nabil, and Harris, Kimberly at el 1243-1254). According to the literature review, authors found out that P53 protein found in a DNA plays an important role in the regulation of transcription and the suppression of tumor cells (1243). According to the authors, this is done through a process known as apoptosis which is a self-mediated cell dead that is natural (1243). The P53 as a DNA protein does its role by regulation of cellular division either via mitosis or meiosis and by doing so; it acts as a checkpoint for cellular division. This prevents any further abnormal cell division which helps in the control of cancer cells multiplication.
Objectives of the Study
The authors sort to investigate two major objectives in this study. The first objective was to determine the significance of acetylation in the functioning of the p53 protein (1243). The second objective was to investigate the mechanism that is deployed by acetylation in influencing the activities that are carried out by p53 (2043).
The Purpose of the Study
The purpose of this study was to determine the effect of substitution of the acetylation sites of p53 on transcriptional activation and the arrest of the cycle of cell division and multiplication. The researchers intended to investigate the effect that such a substitution will play in the activation of transcription and the arrest of the cell cycle.
The Key Observational Findings in the Study
The study found out that acetylation plays an important role in the modification of the functions of p53 (1244). It was unearthed that acetylation is required in not only the activation of p53 but also the activation of p21 gene (1244). The findings were also positive on the arrest of the cell cycle (1244). In addition to that, the results found out that the mechanism used by acetylation to regulate the functions of p53 is by the recruitment of coactivators which is achieved through the physical interactions that do exist between them.
The Techniques Used in the Study
The study employed an experimental study design in which two important techniques were carried out (1244). The first technique that was deployed was the substitution of lysine amino acid with arginine amino acid. The arginine was introduced to maintain the structural component of DNA.Lysine was chosen as the site to be substituted since this is the site that is responsible for the acetylation of P53. Wild-type p53 and the p53 were introduced into the bacteria and then purification was done to attain apparent homogeneity or the similarity that is required or the parent p53. Electrophoresis was used to determine the DNA binding activity (1244). Finally, wild-type p53 was subjected to acetylation in order to investigate the objective.
The Contribution of the Study to the Advancement of Knowledge
According to the authors, the study found out that substitution of the acetylation sites did not reduce the transcription of p53 as previous thought (1254) hence it gave room for more studies to be done about the same in order to provide more knowledge on what regulates transcription as it is clearly shown in this study that acetylation has little effect if any if this experimental study is anything to go critically review.
The study finds out that acetylation plays a role in the arrest of the cell cycle but does not play a role in the transcriptional process of cells.
The results of the experiment are convincing in my own view. The methodology is convincing considering that it was experimental rather than subjective. The other option to carry this experiment is to use another amino acid other than arginine to test the result. I am of the view that the results will be the same.
Barlev, Nickolai, Chehab, Nabil, and Harris, Kimberly at el. Acetylation of p53 Activates Transcription through Recruitment of Coactivators/Histone Acetyltransferases. Journal of Molecular Cell Biology, vol. 8, December 2001, pp. 1243-1254