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Reversible modification of histone tails is a regulatory step in chromatin remodeling. The N-terminal tails of histones are signaling platforms that carry amino acid residues for post-translational modification and contribute to chromosomal higher order structure. These modifications are performed by a number of chromatin modulators such as histone (h) acetyltransferase, h-deacetylase, h-methyltransferase and h-kinase. Large numbers of these enzymes as well as other chromatin-associated proteins share the bromodomain, a signature protein motif. Structural studies reveal not only wide structural conservation of bromodomains but also envision a possible role of this domain in the recognition of specific modified residues in the histone tails. The widespread presence of bromodomains in leukemogenic and cancer genes has provided a fundamental tool for studies of the role of epigenetic and chromatin remodeling in malignant diseases.
Saccharomyces cerevisiae Proteins, Oncogene Proteins, Fusion, Sequence Homology, Amino Acid, Transcription, Genetic, Lysine, Molecular Sequence Data, leukemia, Bromodomain, Nuclear Proteins, lymphoma, Chromatin, Protein Structure, Tertiary, Acetyltransferases, Neoplasms, Mutation, chromatin, Animals, Humans, Amino Acid Sequence, 3D-structure, Histone Acetyltransferases
Saccharomyces cerevisiae Proteins, Oncogene Proteins, Fusion, Sequence Homology, Amino Acid, Transcription, Genetic, Lysine, Molecular Sequence Data, leukemia, Bromodomain, Nuclear Proteins, lymphoma, Chromatin, Protein Structure, Tertiary, Acetyltransferases, Neoplasms, Mutation, chromatin, Animals, Humans, Amino Acid Sequence, 3D-structure, Histone Acetyltransferases
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