Literature search services are currently unavailable. During our hosting provider's UPS upgrade we experienced a hardware failure and are currently working to resolve the issue.

Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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

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.

Pubmed ID: 12535539


  • Wood A
  • Krogan NJ
  • Dover J
  • Schneider J
  • Heidt J
  • Boateng MA
  • Dean K
  • Golshani A
  • Zhang Y
  • Greenblatt JF
  • Johnston M
  • Shilatifard A


Molecular cell

Publication Data

January 21, 2003

Associated Grants

  • Agency: NCI NIH HHS, Id: 1R01CA089455

Mesh Terms

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