Sergey Korolev, Ph.D.
Structure-functional studies of DNA recombination, replication and repair proteins.
Office: DRC, Room 511
Voice: (314) 977-9261
Ph.D., 1993 Engelhardt Institute of Biochemistry and Molecular Biology, Moscow, Russian Academy of Sciences
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.
- A dual role for mycobacterial RecO in RecA-dependent homologous recombination and RecA-independent single-strand annealing.
Gupta R, 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.