The Rad51/RadA N-Terminal Domain Activates Nucleoprotein Filament ATPase Activity

Vitold E. Galkin, Yan Wu, Xiao Ping Zhang, Xinguo Qian, Yujiong He, Xiong Yu, Wolf Dietrich Heyer, Yu Luo, Edward H. Egelman

Research output: Contribution to journalArticle

50 Scopus citations

Abstract

Proteins in the RecA/RadA/Rad51 family form helical filaments on DNA that function in homologous recombination. While these proteins all have the same highly conserved ATP binding core, the RadA/Rad51 proteins have an N-terminal domain that shows no homology with the C-terminal domain found in RecA. Both the Rad51 N-terminal and RecA C-terminal domains have been shown to bind DNA, but no role for these domains has been established. We show that RadA filaments can be trapped in either an inactive or active conformation with respect to the ATPase and that activation involves a large rotation of the subunit aided by the N-terminal domain. The G103E mutation within the yeast Rad51 N-terminal domain inactivates the filament by failing to make proper contacts between the N-terminal domain and the core. These results show that the N-terminal domains play a regulatory role in filament activation and highlight the modular architecture of the recombination proteins.

Original languageEnglish (US)
Pages (from-to)983-992
Number of pages10
JournalStructure
Volume14
Issue number6
DOIs
StatePublished - Jun 2006

Keywords

  • DNA

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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  • Cite this

    Galkin, V. E., Wu, Y., Zhang, X. P., Qian, X., He, Y., Yu, X., Heyer, W. D., Luo, Y., & Egelman, E. H. (2006). The Rad51/RadA N-Terminal Domain Activates Nucleoprotein Filament ATPase Activity. Structure, 14(6), 983-992. https://doi.org/10.1016/j.str.2006.04.001