Homologous pairing and ring and filament structure formation activities of the human Xrcc2·Rad51D complex

Hitoshi Kurumizaka, Shukuko Ikawa, Maki Nakada, Rima Enomoto, Wataru Kagawa, Takashi Kinebuchi, Mitsuyoshi Yamazoe, Shigeyuki Yokoyama, Takehiko Shibata

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Abstract

The Xrcc2 and Rad51D/Rad51L3 proteins, which belong to the Rad51 paralogs, are required for homologous recombinational repair (HRR) in vertebrates. The Xrcc2 and Rad51D/Rad51L3 genes, whose products interact with each other, have essential roles in ensuring normal embryonic development. In the present study, we coexpressed the human Xrcc2 and Rad51D/Rad51L3 proteins (Xrcc2 and Rad51D, respectively) in Escherichia coli, and purified the Xrcc2·Rad51D complex to homogeneity. The Xrcc2·Rad51D complex catalyzed homologous pairing between single-stranded and double-stranded DNA, similar to the function of the Xrcc3· Rad51C complex, which is another complex of the Rad51 paralogs. An electron microscopic analysis showed that Xrcc2·Rad51D formed a multimeric ring structure in the absence of DNA. In the presence of ssDNA, Xrcc2·Rad-51D formed a filamentous structure, which is commonly observed among the human homologous pairing proteins, Rad51, Rad52, and Xrcc3·Rad51C.

Original languageEnglish
Pages (from-to)14315-14320
Number of pages6
JournalJournal of Biological Chemistry
Volume277
Issue number16
DOIs
Publication statusPublished - 2002 Apr 19
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Kurumizaka, H., Ikawa, S., Nakada, M., Enomoto, R., Kagawa, W., Kinebuchi, T., Yamazoe, M., Yokoyama, S., & Shibata, T. (2002). Homologous pairing and ring and filament structure formation activities of the human Xrcc2·Rad51D complex. Journal of Biological Chemistry, 277(16), 14315-14320. https://doi.org/10.1074/jbc.M105719200