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Submitted on July 26, 2006
Developmental and Cell Biology, Centro de Investigaciones Biológicas, Madrid 28040
Corresponding Author: mvidal{at}cib.csic.es
Ring1B/Rnf2 is a RING finger protein member of the Polycomb group (PcG) of proteins, which form chromatin modifying complexes essential for embryonic development and stem cell renewal and which are commonly deregulated in cancer. Ring1B/Rnf2 is a ubiquitin E3 ligase which catalyzes the monoubiquitylation of the histone H2A, one of the histone modifications needed for the transcriptional repression activity of the PcG of proteins. Ring1B/Rnf2 was shown to be part of two complexes, the PRC1 PcG complex and the E2F6.com-1 complex which also contains non-PcG members, thus raising the prospect for additional Ring1B/Rnf2 partners and functions extending beyond the PcG. Here, we used a high-throughput proteomic approach based on the single-step purification, using streptavidin beads, of in vivo biotinylated Ring1B/Rnf2 and associated proteins from a nuclear extract from erythroid cells and their identification by mass spectrometry. About 50 proteins were confidently identified, of which 20 had not been identified previously as subunits of Ring1B/Rnf2 complexes. We found that histone demethylases LSD1/Aof2 and Fbxl10/Jmjd1B, casein kinase 2 subunits and the BcoR corepressor were amongst the new interactors identified. We also isolated a Fbxl10/Jmjd1B complex by biotinylation tagging in order to identify shared interacting partners with Ring1B/Rnf2. In this way we identified a novel Ring1B-Fbxl10 complex which also includes BcoR, CK2{a}, Skp1 and Nspc1/Pcgf1. The putative enzymatic activities and protein interaction and chromatin binding motifs present in this novel Ring1B-Fbxl10 complex provide potentially additional mechanisms for chromatin modification/recruitment to chromatin and more evidence for Ring1B/Rnf2 activities beyond those typically associated with PcG function. Lastly, this work demonstrates the utility of biotinylation tagging for the rapid characterization of complex mixtures of multi-protein complexes achieved through the iterative use of this simple yet high-throughput proteomic approach.
Revised on February 9, 2007
Accepted on February 11, 2007
Proteomic analysis of Ring1B/Rnf2 interactors identifies a novel complex with the Fbxl10/ Jmjd1B histone demethylase and the BcoR corepressor
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