The bromodomain: a chromatin browser?

Front Biosci. 2001 Aug 1:6:D866-76. doi: 10.2741/filetici.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetyltransferases / chemistry
  • Acetyltransferases / metabolism
  • Amino Acid Sequence
  • Animals
  • Chromatin / genetics
  • Chromatin / metabolism*
  • Histone Acetyltransferases
  • Humans
  • Lysine / analogs & derivatives*
  • Lysine / metabolism
  • Molecular Sequence Data
  • Mutation
  • Neoplasms / genetics
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / physiology*
  • Oncogene Proteins, Fusion / physiology
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid
  • Transcription, Genetic

Substances

  • Chromatin
  • Nuclear Proteins
  • Oncogene Proteins, Fusion
  • Saccharomyces cerevisiae Proteins
  • N(alpha)-acetyllysine
  • Acetyltransferases
  • Histone Acetyltransferases
  • Lysine