Edward A. Doisy Department of Biochemistry
Education
Ph.D., 1993 Engelhardt Institute of Biochemistry and Molecular Biology, Moscow, Russian Academy of Sciences
Research Interests
Our lab studies the mechanism of protein function at the atomic resolution level utilizing X-ray crystallography and biochemical approaches. The main focus is recombination mediator proteins (RMPs), which are essential for genome stability and DNA repair in all organisms.
Recent Publications
  • A dual role for mycobacterial RecO in RecA-dependent homologous recombination and RecA-independent single-strand annealing.Ryzhikov M, et al. Nucleic Acids Res. (2013) 41(4):2284-95.
  • Structural studies of SSB iInteraction with RecO.
    Ryzhikov M and Korolev S. Methods Mol Biol. (2012) 922:123-31.
  • Plasmodium falciparum SSB tetramer wraps single-stranded DNA with similar topology but opposite polarity to E. coli SSB.
    Antony E, Weiland EA, et al. J Mol Biol. (2012) 420(4-5):269-83.
  • SSB functions as a sliding platform that migrates on DNA via reptation.
    Zhou R, Kozlov AG, et al. Cell. (2011) 146(2):222-32.
  • Rotations of the 2B sub-domain of E. coli UvrD helicase/translocase coupled to nucleotide and DNA binding.
    Jia H, Korolev S, et al. J Mol Biol. (2011) 411(3):633-48.
  • Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein.
    Ryzhikov M, Postnov D, et al. Nucleic Acids Res. (2011) 39(14):6305-14.
  • The loop-less tmCdc34 E2 mutant defectie in polyubiquitination in vitro and in vivo supports yeast growth in a manner dependent on Ubp14 and Cka2.
    Lass A, Cocklin R, et al. Cell Div. (2011) 6(1):7.