Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain

Article Abstract:

The p53 tumor suppressor's capability to act as a sequence-specific DNA-binding transcription factor enables it to perform antiproliferation. A study was conducted to prove that in vivo and in vitro acetylation may be applied to modify the p53. Results show that the tumor suppressor's sequence-specific DNA-binding function is stimulated by acetylation. Results also reveal the molecular mechanisms involved in the acetyltransferase-containing transcriptional coactivators.

Genetic transcription, Transcription (Genetics), Tumor suppressor genes, DNA binding proteins

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Human TAF(sub II)28 and TAF(sub II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family

Article Abstract:

A study was conducted to characterize the human TATA-binding protein-associated factor (hTAF(sub II))28/hTAF(sub II)18 heterodimer support a histone-like pair in the TFIID complex. The PSI-BLAST program was utilized to carry out general database searches while the coding sequence of the heterodimer residues were amplified by polymerase chain reaction. Results indicated that TAF(sub II)28 and TAF(sub II)18 interact via a canonical histone fold.

Usage, Polymerase chain reaction

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Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53

Article Abstract:

A study defining diverse cofactor functions, as well as underlying mechanisms involving distinct histone modifications, in p53-dependent gene activation is presented. The role for acetyltransferase p300/CBP in p53 function, systems reconstituted with recombinant chromatin templates and (co)activators are elaborated and used to demonstrate the additional involvement of protein arginine methyltransferases PRMT1 and CARM1 in p53 function.

Science & research, Methyltransferases

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