Current Projects
• Investigate the functional contributions of protein subunits to substrate recognition by archaeal RNase P RNA using single-molecule fluorescence-based techniques [collaboration with Dr. Michael G. Poirier (OSU)]
Education and Training
Postdoctoral Researcher – The Ohio State University (Columbus, OH)
• 2019-2020 OSU Center for RNA Biology (CRB) Researcher
• 2020-2022 Pelotonia Postdoctoral Research Fellow
Ph.D. – The Ohio State University (Columbus, OH)
• Program: Ohio State Biochemistry Program
• Advisor: Dr. Zucai Suo
• Dissertation: Kinetic characterization of human DNA polymerase Ε
B.S. – The Ohio State University (Columbus, OH)
• Major: Biochemistry
• Advisor: Dr. Zucai Suo
• Thesis: Characterization of replicative and error-prone DNA polymerases
Undergraduate Research Assistant – The Ohio State University (Columbus, OH)
• Department: Biochemistry
• Advisor: Dr. Zhengrong Wu
• Cloned, overexpressed, and purified mutants of a nucleotide hydrolase (RCL) for biochemical studies aimed at defining its mechanism of action
Publications
• Kimsey IJ°, Szymanski ES°, Zahurancik WJ, Shakya A, Xue Y, Chu CC, Sathyamoorthy B, Suo Z*, and Al-Hashimi HM*. (2018) Dynamic basis for dG•dT misincorporation via tautomerization and ionization. Nature, 554: 195-201. °joint first authors
• Campbell BB°, Light N°, Fabrizio D, Zatzman M, Fuligni F, de Borja R, Davidson S, Edwards M, Elvin JA, Hodel KP, Zahurancik WJ, Suo Z, Lipman T, Wimmer K, Kratz CP, Bowers DC, Laetsch TW, Dunn GP, Johanns TM, Grimmer MR, Smirnov IV, Larouche V, Samuel D, Bronsema A, Osborn M, Stearns D, Raman P, Cole KA, Storm PB, Yalon M, Opocher E, Mason G, Thomas GA, Sabel M, George B, Ziegler DS, Lindhort S, Issai VM, Constantini S, Toledano H, Elhasid R, Farah R, Dvir R, Dirks P, Huang A, Galati MA, Chung J, Ramaswamy V, Irwin MS, Aronson M, Durno C, Taylor MD, Rechavi G, Maris JM, Bouffet E, Hawkins C, Costello JF, Meyn MS, Pursell ZF, Malkin D, Tabori U*, and Shlien A*. (2017) Comprehensive analysis of hypermutation in human cancer. Cell, 171: 1042-1056.e10. °joint first authors
• Wu J, Wang P, Li L, Williams NL, Ji D, Zahurancik WJ, You C, Wang J, Suo Z, and Wang Y. (2017) Replication studies of carboxymethylated DNA lesions in human cells. Nucleic Acids Res., 45: 7276-7284.
• Vyas R, Reed AJ, Raper AT, Zahurancik WJ, Wallenmeyer PC, and Suo Z*. (2017) Structural basis for the D-stereoselectivity of human DNA polymerase ß. Nucleic Acids Res., 45: 6228-6237.
• Tokarsky EJ, Gadkari VV, Zahurancik WJ, Malik CK, Basu AK, and Suo Z*. (2016) Pre-steady-state kinetic investigation of bypass of a bulky guanine lesion by human Y-family DNA polymerases. DNA Repair (Amst.), 46: 20-28.
• Dunn MR, Larsen AC, Zahurancik WJ, Fahmi NE, Meyers M, Suo Z, and Chaput JC*. (2015) DNA polymerase-mediated synthesis of unbiased threose nucleic acid (TNA) polymers requires 7-deazaguanine to suppress G:G mispairing during TNA transcription. J. Am. Chem. Soc., 137: 4014-4017.
• Zahurancik WJ, Baranovskiy AG, Tahirov TH, and Suo Z*. (2015) Comparison of the kinetic parameters of the truncated catalytic subunit and holoenzyme of human DNA polymerase Ε. DNA Repair (Amst.), 29: 16-22.
• Zahurancik WJ, Klein SJ, and Suo Z*. (2014) Significant contribution of the 3’→5′ exonuclease activity to the high fidelity of nucleotide incorporation catalyzed by human DNA polymerase Ε. Nucleic Acids Res., 42: 13853-13860.
• Vyas R°, Zahurancik WJ°, and Suo Z*. (2014) Structural basis for the binding and incorporation of nucleotide analogs with L-stereochemistry by human DNA polymerase Λ. Proc. Natl. Acad. Sci. USA, 111: E3033-3042. °joint first authors
• Zahurancik WJ, Klein SJ, and Suo Z*. (2013) Kinetic mechanism of DNA polymerization catalyzed by human DNA polymerase Ε. Biochemistry, 52: 7041-7049.
• Göksenin AY, Zahurancik WJ, LeCompte KG, Taggart DJ, Suo Z, and Pursell ZF*. (2012) Human DNA polymerase Ε is able to efficiently extend from multiple consecutive ribonucleotides. J. Biol. Chem., 287: 42675-42684.
• Doddapaneni K, Zahurancik W, Haushalter A, Yuan C, Jackman J, and Wu Z. (2011) RCL hydrolyzes 2′-deoxyribonucleoside 5′-monophosphate via formation of a reaction intermediate. Biochemistry, 50: 4712-4719.