Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter

Mol Cell. 2003 Jan;11(1):267-74. doi: 10.1016/s1097-2765(02)00802-x.

Abstract

Ubiquitination of histone H2B catalyzed by Rad6 is required for methylation of histone H3 by COMPASS. We identified Bre1 as the probable E3 for Rad6's role in transcription. Bre1 contains a C3HC4 (RING) finger and is present with Rad6 in a complex. The RING finger of Bre1 is required for ubiquitination of histone H2B, methylation of lysine 4 and 79 of H3 and for telomeric silencing. Chromatin immunoprecipitation experiments indicated that both Rad6 and Bre1 are recruited to a promoter. Bre1 is essential for this recruitment of Rad6 and is dedicated to the transcriptional pathway of Rad6. These results suggest that Bre1 is the likely E3 enzyme that directs Rad6 to modify chromatin and ultimately to affect gene expression.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Gene Silencing
  • Histones / metabolism
  • Ligases / genetics
  • Ligases / metabolism*
  • Lysine / metabolism
  • Methylation
  • Molecular Sequence Data
  • Open Reading Frames
  • Promoter Regions, Genetic*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sequence Alignment
  • Telomere / metabolism
  • Ubiquitin / metabolism
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligases

Substances

  • Histones
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin
  • RAD6 protein, S cerevisiae
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligases
  • Ligases
  • Lysine