Keeping it in the family: diverse histone recognition by conserved structural folds

Crit Rev Biochem Mol Biol. 2010 Dec;45(6):488-505. doi: 10.3109/10409238.2010.512001. Epub 2010 Oct 6.

Abstract

Epigenetic regulation of gene transcription relies on an array of recurring structural domains that have evolved to recognize post-translational modifications on histones. The roles of bromodomains, PHD fingers, and the Royal family domains in the recognition of histone modifications to direct transcription have been well characterized. However, only through recent structural studies has it been realized that these basic folds are capable of interacting with increasingly more complex histone modification landscapes, illuminating how nature has concocted a way to accomplish more with less. Here we review the recent biochemical and structural studies of several conserved folds that recognize modified as well as unmodified histone sequences, and discuss their implications on gene expression.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Acetylation
  • Animals
  • Chromatin Assembly and Disassembly*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Epigenesis, Genetic
  • Gene Expression Regulation
  • Histones / chemistry*
  • Histones / genetics
  • Histones / metabolism*
  • Humans
  • Methylation
  • Phosphorylation
  • Protein Folding
  • Protein Processing, Post-Translational*
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / metabolism*
  • Regulatory Elements, Transcriptional
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism
  • Transcription, Genetic

Substances

  • DNA-Binding Proteins
  • Histones
  • RNA-Binding Proteins
  • Transcription Factors