TY - JOUR
T1 - Identification of the polypyrimidine tract binding protein-associated splicing factor·p54(nrb) complex as a candidate DNA double-strand break rejoining factor
AU - Bladen, Catherine L.
AU - Udayakumar, Durga
AU - Takeda, Yoshihiko
AU - Dynan, William S.
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2005/2/18
Y1 - 2005/2/18
N2 - 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.
AB - 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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U2 - 10.1074/jbc.M412758200
DO - 10.1074/jbc.M412758200
M3 - Article
C2 - 15590677
AN - SCOPUS:14044257206
SN - 0021-9258
VL - 280
SP - 5205
EP - 5210
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 7
ER -