Bromodomain: an acetyl-lysine binding domain

FEBS Lett. 2002 Feb 20;513(1):124-8. doi: 10.1016/s0014-5793(01)03309-9.


Bromodomains, an extensive family of evolutionarily conserved protein modules originally found in proteins associated with chromatin and in nearly all nuclear histone acetyltransferases, have been recently discovered to function as acetyl-lysine binding domains. More recent structural studies of bromodomain/peptide ligand complexes have enriched our understanding of differences in ligand selectivity of bromodomains. These new findings demonstrate that bromodomain/acetyl-lysine recognition can serve as a pivotal mechanism for regulating protein-protein interactions in numerous cellular processes including chromatin remodeling and transcriptional activation, and reinforce the concept that functional diversity of a conserved protein modular structure is achieved by evolutionary changes of amino acid sequences in the ligand binding site.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Acetylation
  • Acetyltransferases / chemistry*
  • Acetyltransferases / metabolism
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Chromatin / chemistry*
  • Chromatin / metabolism
  • Conserved Sequence
  • Evolution, Molecular
  • Gene Products, tat / chemistry
  • Gene Products, tat / metabolism
  • HIV-1
  • Histone Acetyltransferases
  • Humans
  • Lysine / analogs & derivatives*
  • Lysine / metabolism
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Saccharomyces cerevisiae Proteins*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism
  • tat Gene Products, Human Immunodeficiency Virus


  • BDF1 protein, S cerevisiae
  • Chromatin
  • Gene Products, tat
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • tat Gene Products, Human Immunodeficiency Virus
  • Acetyltransferases
  • Histone Acetyltransferases
  • Lysine