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INTS3 controls the hSSB1-mediated DNA damage response

¹ Howard Hughes Medical Institute and ² Department of Pathology, New York University Cancer Institute, New York University School of Medicine, New York, NY 10016
³ Queensland Institute of Medical Research, Herston, Queensland 4006, Australia
⁴ Stowers Institute for Medical Research, Kansas City, MO 64110

Correspondence to Michele Pagano: michele.pagano{at}nyumc.org

Human SSB1 (single-stranded binding protein 1 [hSSB1]) was recently identified as a part of the ataxia telangiectasia mutated (ATM) signaling pathway. To investigate hSSB1 function, we performed tandem affinity purifications of hSSB1 mutants mimicking the unphosphorylated and ATM-phosphorylated states. Both hSSB1 mutants copurified a subset of Integrator complex subunits and the uncharacterized protein LOC58493/c9orf80 (henceforth minute INTS3/hSSB-associated element [MISE]). The INTS3–MISE–hSSB1 complex plays a key role in ATM activation and RAD51 recruitment to DNA damage foci during the response to genotoxic stresses. These effects on the DNA damage response are caused by the control of hSSB1 transcription via INTS3, demonstrating a new network controlling hSSB1 function.

Abbreviations used in this paper: ATM, ataxia telangiectasia mutated; HR, homologous recombination; MISE, minute INTS3/hSSB-associated element; NHF, normal human fibroblast; NSAF, normalized spectral abundance factor; OB, oligonucleotide/oligosaccharide binding; snRNA, small nuclear RNA.

© 2009 Skaar et al.
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