Translating the histone code into leukemia

• Published in: Journal of cellular biochemistry Vol. 96; no. 5; pp. 938 - 950
• Main Authors: Linggi, Bryan E., Brandt, Stephen J., Sun, Zu-Wen, Hiebert, Scott W.
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 01-12-2005
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Animals; chromatin; Chromatin - chemistry; Chromosomes - ultrastructure; Core Binding Factor Alpha 2 Subunit - metabolism; deacetylase; DNA-Binding Proteins - metabolism; Histone Acetyltransferases - metabolism; Histone Deacetylases - chemistry; histones; Histones - chemistry; Histones - metabolism; Humans; Leukemia; Leukemia - genetics; Leukemia - metabolism; Leukemia - pathology; methyltransferase; Models, Biological; Models, Molecular; Molecular Sequence Data; Protein Structure, Tertiary; Proto-Oncogene Proteins c-bcl-6; Recombinant Fusion Proteins - chemistry; Translocation, Genetic
• ISSN: 0730-2312; 1097-4644
• DOI: 10.1002/jcb.20604

The “histone code” is comprised of the covalent modifications of histone tails that function to regulate gene transcription. The post‐translational modifications that occur in histones within the regulatory regions of genes include acetylation, methylation, phosphorylation, ubiquitination, sumoylation, and ADP‐ribosylation. These modifications serve to alter chromatin structure and accessibility, and to act as docking sites for transcription factors or other histone modifying enzymes. Several of the factors that are disrupted by chromosomal translocations associated with hematological malignancies can alter the histone code in a gene‐specific manner. Here, we discuss how the histone code may be disrupted by chromosomal translocations, either directly by altering the activity of histone modifying enzymes, or indirectly by recruitment of this type of enzyme by oncogenic transcription factors. These alterations in the histone code may alter gene expression pattern to set the stage for leukemogenesis. J. Cell. Biochem. © 2005 Wiley‐Liss, Inc.