University of Connecticut
Department of Molecular & Cell Biology
91 North Eagleville Road, Unit 3125
Biology/Physics Building 204
Storrs, CT 06269-3125
Education: Ph.D. University of Iowa, Postdoc Research HHMI/UMDNJ-RWJMS, Piscataway, NJ
Research Interests: Bacteria use an elegant interplay of cellular systems to evaluate their environment and to ensure precise coordination of virulence events. In addition, they have developed clever strategies to avoid host defense mechanisms and guarantee their survival. Consequently, antimicrobial resistance is an increasing concern in the health field, resulting in the demand for new discovery targets and strategies. GTPases are one of the largest and most functionally diverse groups of proteins represented in genomes. Studies have focused primarily on eukaryotic GTPases. Their prokaryotic counterparts, whose functions are essential to numerous cellular processes such as cell viability, protein synthesis and pathogenesis, are not well understood. The goal of my research is to use genetic, biochemical and structural methodologies to study novel families of bacterial GTPases, which have potential as targets for antimicrobial development.
Brown, R.S., Every, A. E., deLivron, M.A. and Robinson, V.L. (2011) Structural analysis of the translation factor BipA reveals a novel ribosome binding domain. under review.
Sheftic, S.R., Garcia, P.P., Robinson, V.L., Gage, D.J. and Alexandrescu, A.T. (2011) NMR Assignments for the Sinorhizobium meliloti Response Regulator Sma0114. Biomol. NMR Assign., 5:55-58.
Barbieri, C.M., Mack, T.R., Robinson, V.L., Miller, M and Stock, A.M. (2010) Regulation of response regulator autophosphorylation through interdomain contacts. J. Biol. Chem., 285:32325-35, paper of the week
deLivron, M.A., Makanji, H.S., Lane, M.C. and Robinson, V.L. (2009) A novel domain in translational GTPase BipA mediates interaction with the 70S ribosome and influences GTP hydrolysis. Biochemistry 48:10533-41.
Rosby, R., Cui, Z., Rogers, E., deLivron, M.A., Robinson, V.L. and DiMario,, P.J. (2009) Knockdown of the Drosophila GTPase, Nucleostemin 1, Impairs Large Ribosomal Subunit Biogenesis, Cell Growth, and Midgut Precursor Cell Maintenance. Mol. Biol. Cell. 20:4424-34.
Guhaniyogi, J., Robinson, V.L. and Stock, A.M. (2006) Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation. J. Mol. Biol. 359:624-45.
Brown, R.A., deLivron, M.A. and Robinson, V.L. (2008) Structure of BipA Reveals a Unique C-terminal Domain, J. Mol. Biol., submitted
Robinson, V.L., Smith, B. and Arnone, A. (2003) A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin. Biochemistry 42: 10113-25.
Robinson, V.L., Wu, T. and Stock, A.M. (2003) Structural Analysis of the interdomain interface of DrrB, An OmpR/PhoB family member from Thermotoga maritima. J. Bacteriol. 185: 4186-94. Special Issue “Structural Biology of Prokaryotes”.
Robinson, V.L., Hwang, J., Fox., E., Inouye., M. and Stock, A.M. (2002) Domain arrangement of Der, a switch protein containing two GTPase domains. Structure 10: 1649-58.
Stock, A.M., Robinson, V.L. and Goudreau, P.N. (2000) Two-component signal transduction. Ann. Rev. Biochem. 69: 183-215.
Robinson, V.L., Buckler, D.R. and Stock, A.M. (2000) A tale of two components: a novel kinase and a regulatory switch. Nat Struct. Biol. 7: 626-33.
Robinson, V.L. and A.M. Stock, A.M. (1999) High energy exchange: Proteins that make or break phosphoramidate bonds. Structure 7: R47-R53.