Zucai Suo PhD

Zucai Suo PhD
ProfessorCollege of Arts & Sciencessuo.3@osu.edu
880 Bioscience Building 484 W 12th Avenue Columbus Ohio 43210
Phone:614-688-3706Fax: (614) 292-6773
  • Non-Member

General Research Interest

Employing advanced enzymology to investigate DNA polymerases, kinases, and proteases.

Research Description

The three major research projects in the Suo laboratory are: 1) using pre-steady state kinetic techniques (rapid chemical quench flow and stopped flow) and single molecule methods to elucidate kinetic mechanisms for DNA polymerases, kinases, and proteases; 2) develop small molecules to inhibit hepatitis C infections; and 3) investigate the efficacy and toxicity of antiviral and anticancer nucleoside analogs.

Transinstitutional Work

We have collaborated with the following groups in the past several years: Dr. Hong Ling, an X-ray Crystallographer at University of Western Ontario, Canada; Dr. John-Stephen Taylor, a chemist at Washington University at St. Louis; and Dr. Ashis Basu, a chemist at University of Connecticut.  

Current Publications

  • Zahurancik WJ, Klein SJ, Suo ZSignificant contribution of the 3'→5' exonuclease activity to the high fidelity of nucleotide incorporation catalyzed by human DNA polymerase ϵNucleic Acids Res in press 11/20/2014
  • Gaur V, Vyas R, Fowler JD, Efthimiopoulos G, Feng JY, Suo ZStructural and kinetic insights into binding and incorporation of L-nucleotide analogs by a Y-family DNA polymerase.Nucleic Acids Res 42 9984-95 11/1/2014
  • Xu C, Maxwell BA, Suo ZConformational Dynamics of Thermus aquaticus DNA Polymerase I during Catalysis.J Mol Biol 426 2901-17 8/12/2014
  • Taggart DJ, Dayeh DM, Fredrickson SW, Suo ZN-terminal domains of human DNA polymerase lambda promote primer realignment during translesion DNA synthesis.DNA Repair (Amst) in press 41-52 8/2/2014
  • Vyas R, Zahurancik WJ, Suo ZStructural basis for the binding and incorporation of nucleotide analogs with L-stereochemistry by human DNA polymerase λ.Proc Natl Acad Sci U S A 111 E3033-42 7/29/2014
  • Suo Z, Taggart DJ, Fredrickson SW, Gadkari VVMutagenic potential of 8-oxo-7,8-dihydro-2'-deoxyguanosine bypass catalyzed by human Y-family DNA polymerases.Chem Res Toxicol 27 931-40 5/19/2014
  • Maxwell BA, Suo ZRecent insight into the kinetic mechanisms and conformational dynamics of Y-Family DNA polymerases.Biochemistry 53 2804-14 5/6/2014
  • Maxwell BA, Xu C, Suo ZConformational dynamics of a Y-family DNA polymerase during substrate binding and catalysis as revealed by interdomain Förster resonance energy transfer.Biochemistry 53 1768-78 3/25/2014
  • Qin Y, Yang Y, Zhang L, Fowler JD, Qiu W, Wang L, Suo Z, Zhong DDirect probing of solvent accessibility and mobility at the binding interface of polymerase (Dpo4)-DNA complex.J Phys Chem A 117 13926-34 12/19/2013
  • Klein SJ, Suo Z, Zahurancik WJKinetic mechanism of DNA polymerization catalyzed by human DNA polymerase ε.Biochemistry 52 7041-9 10/8/2013
  • Espinoza-Herrera SJ, Gaur V, Suo Z, Carey PRFollowing DNA chain extension and protein conformational changes in crystals of a Y-family DNA polymerase via Raman crystallography.Biochemistry 52 4881-90 7/23/2013
  • Maxwell BA, Suo ZSingle-molecule investigation of substrate binding kinetics and protein conformational dynamics of a B-family replicative DNA polymerase.J Biol Chem 288 11590-600 4/19/2013
  • Taggart DJ, Camerlengo TL, Harrison JK, Sherrer SM, Kshetry AK, Taylor JS, Huang K, Suo ZA high-throughput and quantitative method to assess the mutagenic potential of translesion DNA synthesis.Nucleic Acids Res 41 e96 4/1/2013

The Ohio State University Comprehensive Cancer Center – Arthur G. James Cancer Hospital and Richard J. Solove Research Institute (OSUCCC – James) 460 W. 10th Avenue, Columbus, OH 43210 Phone: 1-800-293-5066 | Email: jamesline@osumc.edu