BAIT

BRE1

E3 ubiquitin-protein ligase BRE1, YDL074C
E3 ubiquitin ligase; forms heterodimer with Rad6p to monoubiquinate histone H2B-K123, which is required for the subsequent methylation of histone H3-K4 and H3-K79; required for DSBR, transcription, silencing, and checkpoint control; interacts with RNA-binding protein Npl3p, linking histone ubiquitination to mRNA processing; Bre1p-dependent histone ubiquitination promotes pre-mRNA splicing
Saccharomyces cerevisiae (S288c)
PREY

RPB9

SSU73, DNA-directed RNA polymerase II core subunit RPB9, B12.6, SHI, L000001683, L000001880, YGL070C
RNA polymerase II subunit B12.6; contacts DNA; mutations affect transcription start site selection and fidelity of transcription
Saccharomyces cerevisiae (S288c)

Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Publication

Histone H2B ubiquitylation is associated with elongating RNA polymerase II.

Xiao T, Kao CF, Krogan NJ, Sun ZW, Greenblatt JF, Osley MA, Strahl BD

Rad6-mediated ubiquitylation of histone H2B at lysine 123 has been linked to transcriptional activation and the regulation of lysine methylation on histone H3. However, how Rad6 and H2B ubiquitylation contribute to the transcription and histone methylation processes is poorly understood. Here, we show that the Paf1 transcription elongation complex and the E3 ligase for Rad6, Bre1, mediate an association of ... [more]

Mol. Cell. Biol. Jan. 01, 2005; 25(2);637-51 [Pubmed: 15632065]

Throughput

  • High Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Curated By

  • BioGRID