E2–BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-10

AUTHORS

Devin E Christensen, Peter S Brzovic, Rachel E Klevit

ABSTRACT

An E3 ubiquitin ligase mediates the transfer of activated ubiquitin from an E2 ubiquitin-conjugating enzyme to its substrate lysine residues. Using a structure-based, yeast two-hybrid strategy, we discovered six previously unidentified interactions between the human heterodimeric RING E3 BRCA1-BARD1 and the human E2s UbcH6, Ube2e2, UbcM2, Ubc13, Ube2k and Ube2w. All six E2s bind directly to the BRCA1 RING motif and are active with BRCA1-BARD1 for autoubiquitination in vitro. Four of the E2s direct monoubiquitination of BRCA1. Ubc13-Mms2 and Ube2k direct the synthesis of Lys63- or Lys48-linked ubiquitin chains on BRCA1 and require an acceptor ubiquitin attached to BRCA1. Differences between the mono- and polyubiquitination activities of the BRCA1-interacting E2s correlate with their ability to bind ubiquitin noncovalently at a site distal to the active site. Thus, BRCA1 has the ability to direct the synthesis of specific polyubiquitin chain linkages, depending on the E2 bound to its RING. More... »

PAGES

941-948

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb1295

DOI

http://dx.doi.org/10.1038/nsmb1295

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005317389

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17873885


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