Dr. Luis Cruz-Vera Associate Professor, Biological Sciences Contact 301 Sparkman DriveShelby CenterRoom 369LHuntsville, AL 35899 Campus Map email@example.com Biography My lab is interested in understanding how cellular products modulate the function of ribosomes, the molecular machines that carry out protein production, to influence gene expression, cellular metabolism and phenotypic plasticity in bacterial cells. Cellular protein production can be controlled by diverse mechanisms since a substantial number of factors and events are involved during this process. Despite the diversity, the regulation of protein production keeps two common and essential characteristics: 1) the nature of the synthesized protein plays an important role in the modulation of the function of the ribosome; and 2) inhibition, or delay, in the ribosome function leads to the accumulation of intermediary products of the protein production, named peptidyl-tRNAs. The objective of our research is to identify genes which expression depends in the regulation of the ribosome function by detecting peptidyl-tRNAs expressed under relevant cell growth conditions. Also, determine the molecular mechanism(s) responsible for regulation of the ribosome function by cellular products. We expect to produce a gene-expression profiling technology to analyze in vivo the accumulation of peptidyl-tRNAs. Curriculum Vitae Personal Website Education Postdoctoral fellow department of Biology, Stanford University. 2003-2007 Postdoctoral fellow department of Genetics and Molecular Biology, CINVESTAV-Mexico. 2000-2003 Ph.D in Genetics and Molecular Biology, CINVESTAV-Mexico, 2000 M.S in Genetics and Molecular Biology, CINVESTAV-Mexico, 1996 B.S in Chemistry and Pharmacobiology, BUAP-Mexico, 1995 Expertise Molecular Biology Molecular Biology Microbiology Translation & Gene Expression Regulation Gene Expression Regulation Protein Synthesis Recent Publications Emmanuel, J. S., Gordon, E. R., Sengupta, A., Noble, J.T., and Cruz-Vera, L.R. (2019). The regulatory TnaC nascent peptide preferentially inhibits release factor 2-mediated hydrolysis of peptidyl-tRNA. J. Biol. Chem.294(50): 19224-19235 Martinez, A. K., Gordon, E., Sengupta, A., Shirole, N. H., Klepacki, D., Martinez-Garriga B., Brown L.M., Benedik, M. J., Yanofsky, C., Mankin, A. S., Vazquez-Laslop, N., Sachs, M. S. and Cruz-Vera, L.R.(2014). Interactions of the TnaC nascent peptide with rRNA in the exit tunnel enable the ribosome to respond to free tryptophan. Nucleic Acid Res. 42(2): 1245-1256 Mcfeeters H., Gilbert M.J., Thompson R.M., Setzer, W.N., Cruz-Vera, L.R, McFeeters, R.L. (2012). Inhibition of essential bacterial peptidyl-tRNA hydrolase activity by tropical plant extracts. Nat. Prod. Commun.7(8):1107-1110. Martinez, A. K., Shirole, N. H., Murakami, S., Benedik, M. J., Sachs, M. S. and Cruz-Vera, L.R.(2012). Crucial elements that maintain the interactions between the regulatory TnaCpeptide and the ribosome exit tunnel responsible for Trp inhibition of ribosome function. Nucleic Acid Res. 40(5):2247-2257. Harris S. M., McFeeters H., Ogungbe I. V., Cruz-Vera L. R., Setzer W. N., Jackes B. R., and McFeeters R. L. (2011). Peptidyl-tRNA hydrolase screening combined with molecular docking reveals the antibiotic potential of Syzygium johnsonii bark extract.Nat. Prod. Commun.6(10):1421-1424. Cruz-Vera, L.R., Sachs, M.S., Squires, C.L. and Yanofsky, C .(2011). Nascent polypeptide sequences that influence ribosome function. Curr. Opin. Microbiol. 14(2):160-166. Shirole, N., Balasubramanian, S. and Cruz-Vera, L. R. (2011). Isolation of translating ribosomes containing peptidyl-tRNAs for functional and structural analyses. J. Vis. Exp. DOI: 10.3791/2498. Cruz-Vera, L.R., Yang, R. and Yanofsky, C. (2009). Tryptophan inhibits Proteus vulgaris TnaC leader peptide elongation, activating tna operon expression. J. Bacteriol.191:7001-7006. Yang, R., Cruz-Vera, L.R., and Yanofsky, C. (2009). 23S rRNA nucleotides in the peptidyl transferase center are essential for tryptophanase operon induction. J. Bacteriol.191:3445-3450. Cruz-Vera, L.R. and Yanofsky, C. (2008). Conserved residues Asp16 and Pro24 of TnaC-tRNAPro participate in tryptophan induction of Tna operon expression. J, Bacteriol. 190:4791-4797.