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Association of human RAD52 protein with transcription factors
Biochemical and biophysical research communications
  • J. M. Liu
  • Xiangbing Meng, University of Iowa
  • Z. Y. Shen
Document Type
Peer Reviewed
Publication Date
NLM Title Abbreviation
Biochem Biophys Res Commun
DOI of Published Version
The human RAD52 protein has been implicated in DNA homologous recombination. Four major functional domains have been identified: a DNA binding domain (amino acids 1-85), a self-association and UBC9-interacting domain (amino acids 85-159), an RPA-interacting domain (amino acids 221-280), and a RAD51-interacting domain (amino acids 287-330). However, it is uncertain about the functional roles of the C-terminal region of RAD52 protein. In this report, we demonstrate an association of a C-terminal domain of human RAD52 (amino acids 302-418) with the XPB and XPD subunits of transcription factor TFIIH and RNA polymerase II (RNAPII). Using a Gal-4 binding based transcription assay, we further show that this C-terminal domain activates transcription. However, the RAD52 self-association domain suppresses transcription, resulting in an overall activity of transcriptional suppression by the full-length RAD52 protein. These results suggest a novel activity of RAD52 in transcription regulation and may further imply a functional role of RAD52 in targeting DNA damage on transcription active loci to recombinational repair. (C) 2002 Elsevier Science (USA). All rights reserved.
Published Article/Book Citation
Biochemical and biophysical research communications, 297:5 (2002) pp.1191-1196.
Citation Information
J. M. Liu, Xiangbing Meng and Z. Y. Shen. "Association of human RAD52 protein with transcription factors" Biochemical and biophysical research communications Vol. 297 Iss. 5 (2002) p. 1191 - 1196 ISSN: 0006-291X
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