Hayes, Christopher S - University of California, Santa Barbara

个人简介

Dr. Hayes received his B.A. (Biology) and M.S. (Applied Immunology) degrees from the University of Southern Maine, and his Ph.D. in Molecular Biology & Biochemistry from the University of Connecticut School of Medicine. He was a Walter Winchell-Damon Runyon Cancer Research Fund postdoctoral fellow at the Massachusetts Institute of Technology and joined the MCDB faculty in 2004.

研究领域

The Hayes lab studies the molecular biology and biochemistry of prokaryotic ribonucleases that regulate gene expression and cell growth. The two main research interests revolve around the mechanisms of ribosome rescue and the function of cytotoxic nucleases encoded by contact-dependent growth inhibition (CDI) systems. Bacterial ribosome rescue is mediated by the transfer-messenger RNA (tmRNA) and alternative ribosome rescue (ArfA) quality control systems, which co-operate to maintain active ribosome pools. CDI systems are widely distributed throughout α, β and γ-proteobacteria and function in growth competition. Many of these systems deploy toxic nucleases that are delivered into the cytosol of susceptible target bacteria. We are interested in the mechanisms of nuclease delivery, activation and immunity during CDI.

近期论文

查看导师最新文章（温馨提示：请注意重名现象，建议点开原文通过作者单位确认）

Michalska K, Gucinski GC, Garza-Sánchez F, Johnson PM, Stols LM, Eschenfeldt WH, Babnigg G, Low DA, Goulding CW, Joachimiak A, Hayes CS (2017) Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs. Nucleic Acids Research 45:10306-10320 Ruhe ZC, Nguyen JY, Xiong J, Koskiniemi S, Beck CM, Perkins BR, Low DA, Hayes CS (2017) CdiA effectors use modular receptor-binding domains to recognize target bacteria. mBio 8:e00290-17 Jones AM, Garza-Sánchez F, So J, Hayes CS, Low DA (2017) Activation of contact-dependent antibacterial tRNase toxins by translation elongation factors. Proceedings of the National Academy of Sciences U.S.A. 114:E1951-E1957 Beck, C. M., Willett, J. L. E., Cunningham, D. A., Kim, Jeff J., Low, D. A. and C. S. Hayes (2016) CdiA effectors from uropathogenic Escherichia coli use heterotrimeric osmoporins as receptors to recognize target bacteria. PLOS Pathogens 12:e1005925 Johnson, P. M., Beck, C. M., Morse, R. P., Garza-Sánchez, F., Low, D. A., Hayes, C. S. and C. W. Goulding (2016) Unraveling the essential role of CysK in CDI toxin activation. Proceedings of the National Academy of Sciences U.S.A. 113:9792-9797 Willett, J. L. E., Gucinski, G. C., Fatherree, J., Low, D. A., and C. S. Hayes (2015) Contact-dependent growth inhibition (CDI) toxins exploit multiple independent cell-entry pathways. Proceedings of the National Academy of Sciences U.S.A. 112:11341-11346 Ruhe, Z. C., Townsley, L., Wallace, A. B., King, A., Van der Woude, M. W., Low, D. A., Yildiz, F. H., and C. S. Hayes (2015) CdiA promotes receptor-independent intercellular adhesion. Molecular Microbiology 198:175-192 Beck, C. M., Morse, R. P., Cunningham, D. A., Iniquez, I., Low, D. A., Goulding, C. W. and C. S. Hayes (2014) CdiA from Enterobacter cloacae delivers a toxic ribosomal RNase into target bacteria. Structure 22:707-718 Koskiniemi, S., Garza-Sánchez, F., Sandegren, L., Webb, J. S., Braaten, B., Poole, S. J., Andersson, D. I., Hayes, C. S. and D. A. Low (2014) Selection of orphan Rhs toxin expression in evolved Salmonella enterica serovar Typhimurium. PLoS Genetics 10:e1004255 Ruhe, Z. C., Wallace, A. B., Low, D. A. and C. S. Hayes (2013) Receptor polymorphism restricts contact-dependent growth inhibition to members of the same species. mBio 4:e00480-13 Koskiniemi, S., Lamoureux, J. G., Nikolakakis, K. C., t’Kint de Roodenbeke, C., Kaplan, M. D., Low, D. A. and C. S. Hayes (2013) Rhs proteins from diverse bacteria mediate intercellular competition. Proceedings of the National Academy of Sciences U.S.A. 110:7032-7037 Morse, R., Nikolakakis, K. C., Willett, J. L. E., Gerrick, E., Low, D., A., Hayes, C. S. and C. W. Goulding (2012) Structural basis for toxicity and immunity in contact-dependent growth inhibition (CDI) systems. Proceedings of the National Academy of Sciences U.S.A. 109:21480-21485 Diner, E. J., Beck, C. M., Webb, J. S., Low, D. A., and C. S. Hayes (2012) Identification of a target cell permissive factor required for contact-dependent growth inhibition (CDI). Genes and Development 26:515-525 Poole, S. J., Diner, E. J., Aoki, S. K., Braaten, B. A., Low, D. A., and C. S. Hayes (2011) Identification of functional toxin/immunity genes linked to contact-dependent growth inhibition (CDI) and rearrangement hotspot (Rhs) systems. PLoS Genetics 7:e1002217 Garza-Sánchez, F., Schaub, R. E., Janssen, B. D., and C. S. Hayes (2011) tmRNA regulates synthesis of the ArfA ribosome rescue factor. Molecular Microbiology 80:1204-1219 Aoki, S. K., Diner, E. J., t'Kint de Roodenbeke, C., Burgess, B. R., Poole, S. J., Braaten, B. A., Jones, A. M., Webb, J. S., Hayes, C. S., Cotter, P. A., and D. A. Low (2010) A widespread family of polymorphic contact-dependent toxin delivery systems in bacteria. Nature 468:439-442 Garza-Sánchez, F., Janssen, B. D., and C. S. Hayes (2006) Prolyl-tRNAPro in the A-site of SecM-arrested ribosomes inhibits the recruitment of transfer-messenger RNA. Journal of Biological Chemistry 281:34258-34268 Hayes, C. S., and R. T. Sauer (2003) Cleavage of the A-site mRNA codon during ribosome pausing provides a mechanism for translational quality control. Molecular Cell 12:903-911 Hayes, C. S., Bose, B., and R. T. Sauer (2002) Proline residues at the C-terminus of nascent chains induce SsrA-tagging during translation termination. Journal of Biological Chemistry 277:33825-33832