Expression profile of G9A and p300 in leukemia and
normal blood sample

Abstract

DNA is allied with histone proteins to form nucleosomes and higher order structures available in eukaryotes. Histones having amino termini can be modified by acetylation. Acetylation of explicit residues of the histones is associated with gene activity and may play a elementary role in transcriptional regulation. Bromodomains, motifs found in several eukaryotic transcription factors, exclusively interact with acetyl-lysines in histones H3 and H4. p300 is functionally conserved transcriptional coactivators for various transcription factors and have intrinsic acetyltransferase activity. The covalent alteration of histone tails has regulatory roles in various nuclear processes, such as organization of transcription and mitotic chromosome condensation. Among the different groups of enzymes identified to catalyze the covalent modification, the most topical additions are the histone methyltransferases (HMTases), whose functions are now being characterized. G9A is a novel mammalian HMTase that prefer lysine. Specific chromosome translocations commonly found in human leukemia engross rearrangements of genes which are implicated in the regulation of hematopoiesis. Consequently, the chromosome translocations often results in the expression of gene products.