Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch

Mol Cell. 2000 Aug;6(2):225-31. doi: 10.1016/s1097-2765(00)00024-1.

Abstract

In Tetrahymena, histone H1 phosphorylation can regulate transcription and mimics loss of H1 from chromatin. We investigated the mechanism by which H1 phosphorylation affects transcription. Tetrahymena strains were created containing mutations in H1 that mimicked the charge of the phosphorylated region without mimicking the structure or increased hydrophilicity of the phosphorylated residues. Whenever the charge resembled that of the phosphorylated state, the induced expression of the CyP1 gene was greatly inhibited. Whenever the charge was similar to that of the dephosphorylated state, the CyP1 gene was induced normally. These results argue strongly that phosphorylation of H1 acts by changing the overall charge of a small domain, not by phosphate recognition or by creating a site-specific charge.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Biolistics
  • DNA-Binding Proteins*
  • Fungal Proteins / genetics
  • Gene Expression Regulation*
  • Histones / chemistry
  • Histones / genetics
  • Histones / metabolism*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Phosphorylation
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Tetrahymena thermophila / genetics
  • Tetrahymena thermophila / physiology*
  • Trans-Activators / genetics
  • Transcription Factors
  • Transcription, Genetic

Substances

  • DNA-Binding Proteins
  • Fungal Proteins
  • HAP1 protein, S cerevisiae
  • Histones
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Transcription Factors