Chris received his Ph.D from the University of California at Santa Barbara in 1988. From 1989-1991, he carried out postdoctoral studies with Paul Schimmel, then at M.I.T. He joined the University of Vermont in 1991. He is currently Professor in the Department of Biochemistry, and Adjunct Professor in the Department of Microbiology and Molecular Genetics. Chris also serves as one of the three co-directors of the University of Vermont undergraduate program in Biochemistry.
1995 J. Walter Juckett Scholar Award
1996 College of Medicine Faculty Development Award
2002 Standing Member, NIH Biochemistry Study Section 2002-2005
2004 Chair, Molecular Genetics A Study Section, NIH 2004-2006
2006 Editorial Board, Journal of Biological Chemistry 2006-20102008 NIH Special Emphasis Panel, F31 Fellowships for Minority Graduate Students
Farris, M. & Francklyn, C.S. (2007). Co-factor binding by all retinoic acid resistant mutants of the retinoic acid receptor a from acute promyelocytic leukemia. In revision.
Guth, E. & Francklyn, C.S. (2007). Kinetic discrimination proofreading of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase. Molecular Cell, 25: 531-542.
Champagne, K.S., Piscitelli, E., & Francklyn, C.S. (2006). Substrate recognition by the herto-octameric ATP phosphoribosyltransferase from Lactococcus lactis. Biochemistry, 45(50): 14933-14943.
Champagne KS, Sissler M, Larrabee Y, Doublie S, Francklyn CS. (2005). Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog. J Biol Chem., 280(40):34096-104. view the structure at PDB.
Guth, E., Connolly, S.A., Bovee, M., & Francklyn, C.S. (2005). A substrate assisted concerted mechanism for aminoacylation of tRNAHis by histidul-tRNA sythetase from Escerichia coli. Biochemistry, 44(10): 3785-3795.
Qui, H., Dong, J., Ha, C., Francklyn, C.S., & Hinnebusch, A.G. (2001). The tRNA binding in GCN2 contains a dimerization domain that interacts with the kinase domain and is required for activation by uncharged tRNA. EMBO J., 20: 1425-1438.
Sankaranarayanan, R., Dock-Bregeon, A.C., Rees., Bovee, M., Caillet, J., Romby, P., Francklyn, C.S., & Moras, D. (2000). Zinc Ion Mediated Amino Acid Discrimination by Threonyl-tRNA Synthetase. Nature Structural Biology, 7: 461-465.
Dock-Bregeon, A.C., Sankaranarayan, R., Romby, P., Caillet, J., Springer, M., Rees, B., Francklyn, C.S., Ehresmann, C., Moras, D. (2000). Transfer RNA mediated editing in the Class II Threonyl-tRNA Synthetase: Mirror Image of a Class I Editing Mechanism. Cell, 103:877-884.
Sissler, M., Delorme, C., Bond, J., Ehrlich, S.D., Renault, P., & Francklyn, C. (1999). An aminoacyl-tRNA synthetase progenitor with a catalytic role in amino acid biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 96: 8985-8990.
Guth E, Farris M, Bovee M, Francklyn CS. (2009) Asymmetric amino acid activation by class II histidyl-tRNA synthetase from Escherichia coli. J Biol Chem. 2009 in press. Francklyn, C. & Schimmel, P. (1989) Aminoacylation of RNA Minihelices with Alanine. Nature 337: 478-481.
Francklyn, C., Shi, J. P., & Schimmel, P. (1992) Overlapping Nucleotide Determinants for Specific Aminoacylation of RNA Microhelices with Three Different Amino Acids. Science. 255: 1121-1125.8990.
Dock-Bregeon, A.-C., Sankaranarayan R., Romby, P., Caillet, J., Springer, M., Rees, B., Francklyn, C. S., Ehresmann, C., Moras, D. (2000) Transfer RNA mediated editing in the Class II Threonyl-tRNA Synthetase: Mirror Image of a Class I Editing Mechanism. Cell: 103: 877-884.
Ruan, B., Bovee, M.L., Sacher, M., Stathopoulos, C., Poralla, K., Francklyn, C.S., & Soll, D. (2005) A unique hydrophobic cluster near the active site contributes to differences of borrelidin inhibition among threonyl-tRNA synthetases. J. Biol. Chem. 280: 571-577.
Guth, E. & Francklyn, C.S. (2007) Kinetic Discrimination proofreading of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA Synthetase. Molecular Cell 25:531-542.
Minajigi A, Francklyn CS. (2008) RNA-assisted catalysis in a protein enzyme: the 2´-hydroxyl of tRNA (Thr) promotes aminoacylation by threonyl-tRNA synthetase. Proc. Natl. Acad. Sci. U. S. A. 2008 Nov 18; 105 (46): 17748-53. PMID: 18997014.
Minajigi A, Francklyn CS. (2010) Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase. J. Biol. Chem. Jul 30; 285(31): 23810-7. PMID: 20504770.
Puffenberger EG, Jinks RN, Sougnez C, Cibulskis K, Willert RA, Achilly NP, Cassidy RP, Fiorentini CJ, Heiken KF, Lawrence JJ, Mahoney MH, Miller CJ, Nair DT, Politi KA, Worcester KN, Setton RA, Dipiazza R, Sherman EA, Eastman JT, Francklyn C, Robey-Bond S, Rider NL, Gabriel S, Morton DH, Strauss KA (2012) Genetic mapping and exome sequencing identify variants associated with five novel diseases. PLoS One. 2012;7(1):e28936. Epub 2012 Jan 17. PMID: 22279524.
Williams TF, Mirando AC, Wilkinson, B, Francklyn C, Lounsbury KM. Secreted Threonyl-tRNA Synthetase Stimulates Endothelial Cell Migration and Angiogenesis. (2013) Scientific Reports. 3: 1317 DOI: 10.1.1038/srep01317.
Li L, Francklyn, C., Carter CW Jr. (2013) Aminoacylating Urzymes challenge the RNA world hypothesis. J. Biol. Chem. 288(37) 26856-63. PMID:23867455