Association of human RAD52 protein with transcription factorsBiochemical and biophysical research communications
NLM Title AbbreviationBiochem Biophys Res Commun
DOI of Published Version10.1016/S0006-291X(02)02353-7
AbstractThe 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 CitationBiochemical and biophysical research communications, 297:5 (2002) pp.1191-1196.
Citation InformationJ. 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
Available at: http://works.bepress.com/xiangbing_meng/15/