Self-association of human RAD52 protein

Zhiyuan Shen, Scott R. Peterson, Jarmon C. Comeaux, Devon Zastrow, Robert K. Moyzis, E. Morton Bradbury, David J. Chen

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

The yeast RAD52 protein is required for both homologous DNA recombination and repair of DNA double-strand breaks. RAD52 can bind to the yeast RAD51 protein, which shares a functional similarity with the bacterial RecA protein. The gene encoding the human homolog of the yeast RAD52 protein shares significant N-terminus amino acid homology with the yeast RAD52 protein. Using a yeast two hybrid system and purified GST-RAD52 fusion protein, we demonstrate that the human RAD52 protein self-associates both in vivo and in vitro. The region of RAD52 required for its self-interaction, mapped here as amino acid residues 65-165, has significant homology with the yeast RAD52 (52% identity, and 89% similarity), suggesting the importance of self-association for RAD52's function.

Original languageEnglish (US)
Pages (from-to)81-89
Number of pages9
JournalMutation Research - DNA Repair
Volume364
Issue number2
DOIs
StatePublished - Oct 18 1996

Keywords

  • DNA double-strand breaks
  • DSB
  • RAD51
  • RAD52
  • Two hybrid system

ASJC Scopus subject areas

  • Molecular Biology
  • Toxicology
  • Genetics

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    Shen, Z., Peterson, S. R., Comeaux, J. C., Zastrow, D., Moyzis, R. K., Bradbury, E. M., & Chen, D. J. (1996). Self-association of human RAD52 protein. Mutation Research - DNA Repair, 364(2), 81-89. https://doi.org/10.1016/0921-8777(96)00025-0