Christopher S. Hayes

Biography

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.

Research

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.

Selected Publications

Ruhe, Z. C., Subramanian, P., Song, K., Nguyen, J. Y., Stevens, T. A., Low, D. A., Jenson, G. J., and C. S. Hayes (2018) Programmed secretion arrest and receptor-triggered toxin export during antibacterial contact-dependent growth inhibition. Cell 175:921-933

Michalska, K., Gucinski, G. C., Garza-Sánchez, F., Johnson, P. M., Stols, L., Eschenfeldt, W. H., Babnigg, G., Low, D. A., Goulding, C. W., Joachimiak, A., and C. S. Hayes (2017) Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific tRNAs. Nucleic Acids Research 45:10306-10320

Ruhe, Z. C., Nguyen, J. Y., Xiong, J., Koskiniemi, S, Beck, C. M., Perkins, B. R., Low, D. A. and C. S. Hayes (2017) Toxic CdiA effectors recognize target bacteria using modular receptor-binding domains. mBio 8:e00290-17

Beck, C. M., Willett, J. L. E., Cunningham, D. A., Kim, J. 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

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., Nguyen, J. Y., Beck, C. M., Low, D. A. and C. S. Hayes (2014) The proton-motive force is required for translocation of CDI toxins across the inner membrane of target bacteria. Molecular Microbiology 94:466-481

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., 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

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

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