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

Adam Wood, Nevan J. Krogan, Jim Dover, Jessica Schneider, Jonathan Heidt, Marry Ann Boateng, Kimberly Dean, Ashkan Golshani, Yi Zhang, Jack F. Greenblatt, Mark Johnston, Ali Shilatifard

Research output: Contribution to journalArticlepeer-review

433 Scopus citations

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.

Original languageEnglish
Pages (from-to)267-274
Number of pages8
JournalMolecular Cell
Volume11
Issue number1
DOIs
StatePublished - 1 Jan 2003
Externally publishedYes

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