4r7e | pdb_00004r7e
Structure of Bre1 RING domain
Structural highlights
Function[BRE1_YEAST] E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. Also modulates the formation of double-strand breaks during meiosis.[1] [2] [3] [4] [5] Publication Abstract from PubMedMonoubiquitination 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. Proteins 2015;. (c) 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc. Structure of the yeast Bre1 RING domain.,Kumar P, Wolberger C Proteins. 2015 Apr 9. doi: 10.1002/prot.24812. PMID:25864391[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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