Structure of the yeast Bre1 RING domain

Pankaj Kumar, Cynthia Wolberger

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Monoubiquitination of histone H2B at Lys123 in yeast plays a critical role in regulating transcription, mRNA export, DNA replication, and the DNA damage response. The RING E3 ligase, Bre1, catalyzes monoubiquitination of H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The crystal structure of a C-terminal fragment of Bre1 shows that the catalytic RING domain is preceded by an N-terminal helix that mediates coiled-coil interactions with a crystallographically related monomer. Homology modeling suggests that the human homologue of Bre1, RNF20/RNF40, heterodimerizes through similar coiled-coil interactions.

Original languageEnglish (US)
Pages (from-to)1185-1190
Number of pages6
JournalProteins: Structure, Function and Bioinformatics
Issue number6
StatePublished - Jun 1 2015


  • E2 ubiquitin-conjugating enzyme
  • Histone modification
  • Transcription
  • Ubiquitin
  • X-ray crystallography

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Structure of the yeast Bre1 RING domain'. Together they form a unique fingerprint.

Cite this