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usp, cells, pubmed, fig, article, resection, brca, ubiquitin, google, scholar, dna, cas, supplementary, buffer, nacl, repair, cell, rad, substrate, data, protein, activity, habrcaub, lysis, site, sample, central, cleavage, column, ubiquitinated, ssa, foci, nature, ubiquitination, haub, ligase, purified, expression, healthcare, analysis, loss, expressed, beads, biol, lengths, concentration, function, protease, auxiliary, tris,

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nature portfolio ez-link sulfo-nhs-lc-biotin biomedical research privacy policy swi/snf-related helicase smarcad12 blm-dna2 helicase/endonuclease complexes ice-cold phosphate-buffered saline advertising 400 μm isopropyl β-d-1-thiogalactopyranoside reprints breast cancer-derived mutation resulting single-stranded dna middle nature 477 nature 431 nature 499 nature 449 nature 532 nature histone-h2a-specific ubiquitin ligase hela-flpin egfp-usp48iso1 cells double-strand break repair dna double-strand breaks double-strand dna breaks disruptive zinc-ligating variant single-strand annealing pathway cleaving brca-initiated ubiquitination preventing large-scale rearrangements brca1-bard1-usp48 circuit promotes long-range resection10 usp48-positive laser lines uniprot identifier q86uv5-2/usp48iso2 ring heterodimer brca1-bard1 uncleavable h2a-ub fusion quantified usp48-catalyzed cleavage original author homology-directed dna repair mutagenic single-strand annealing disrupt damage-signaling dependent social media possibly allowing cross-talk brca1–bard1 nucleosome recognition k27-linked di-ubiquitin smarcad1-mediated nucleosome sliding }\frac{{k_{obs\left serum-free insectxpress medium hela-flag-usp48-c98siso2 sided mann–whitney test brdu-sensitized hela cells anti-h2a western blotting

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         description:BRCA1-BARD1-catalyzed ubiquitination of histone H2A is an important regulator of the DNA damage response, priming chromatin for repair by homologous recombination. However, no specific deubiquitinating enzymes (DUBs) are known to antagonize this function. Here we identify ubiquitin specific protease-48 (USP48) as a H2A DUB, specific for the C-terminal BRCA1 ubiquitination site. Detailed biochemical analysis shows that an auxiliary ubiquitin, an additional ubiquitin that itself does not get cleaved, modulates USP48 activity, which has possible implications for its regulation in vivo. In cells we reveal that USP48 antagonizes BRCA1 E3 ligase function and in BRCA1-proficient cells loss of USP48 results in positioning 53BP1 further from the break site and in extended resection lengths. USP48 repression confers a survival benefit to cells treated with camptothecin and its activity acts to restrain gene conversion and mutagenic single-strand annealing. We propose that USP48 promotes genome stability by antagonizing BRCA1 E3 ligase function. BRCA1 ligase activity is tightly regulated to maintain genome stability and confer DNA double strand repair. Here the authors identify USP48 as a H2A deubiquitinating enzyme that acts as a BRCA1 E3 ligase antagonist and characterize its role during DNA repair.
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      headline:USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A
      description:BRCA1-BARD1-catalyzed ubiquitination of histone H2A is an important regulator of the DNA damage response, priming chromatin for repair by homologous recombination. However, no specific deubiquitinating enzymes (DUBs) are known to antagonize this function. Here we identify ubiquitin specific protease-48 (USP48) as a H2A DUB, specific for the C-terminal BRCA1 ubiquitination site. Detailed biochemical analysis shows that an auxiliary ubiquitin, an additional ubiquitin that itself does not get cleaved, modulates USP48 activity, which has possible implications for its regulation in vivo. In cells we reveal that USP48 antagonizes BRCA1 E3 ligase function and in BRCA1-proficient cells loss of USP48 results in positioning 53BP1 further from the break site and in extended resection lengths. USP48 repression confers a survival benefit to cells treated with camptothecin and its activity acts to restrain gene conversion and mutagenic single-strand annealing. We propose that USP48 promotes genome stability by antagonizing BRCA1 E3 ligase function. BRCA1 ligase activity is tightly regulated to maintain genome stability and confer DNA double strand repair. Here the authors identify USP48 as a H2A deubiquitinating enzyme that acts as a BRCA1 E3 ligase antagonist and characterize its role during DNA repair.
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