Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 280, Issue 7, Pages 5205-5210Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M412758200
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Funding
- NCI NIH HHS [R01 CA098239, R01 CA098239-01A2, CA 98239] Funding Source: Medline
- NIGMS NIH HHS [GM 35866] Funding Source: Medline
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The biological effects of ionizing radiation are attributable, in large part, to induction of DNA double-strand breaks. We report here the identification of a new protein factor that reconstitutes efficient double-strand break rejoining when it is added to a reaction containing the five other polypeptides known to participate in the human nonhomologous end-joining pathway. The factor is a stable heteromeric complex of polypyrimidine tract-binding protein-associated splicing factor (PSF) and a 54-kDa nuclear RNA-binding protein (p54(nrb)). These polypeptides, to which a variety of functions have previously been attributed, share extensive homology, including tandem RNA recognition motif domains. The PSF-p54(nrb) complex cooperates with Ku protein to form a functional preligation complex with substrate DNA. Based on structural comparison with related proteins, we propose a model where the four RNA recognition motif domains in the heteromeric PSF-p54(nrb) complex cooperate to align separate DNA molecules.
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