Mark Bayfield

mbayfieldPhD (Brown)
Associate Professor
E–mail: bayfield@yorku.ca
Research areas:  Microbiology, RNA Biology, Biochemistry, Molecular Biology and Genetics

Research Focus

Our research focuses on how conserved mechanisms in RNA metabolism function in both general cellular processes and adaptations to stress.

A major research focus is the La antigen, which is an abundant, ubiquitous factor with several roles in RNA metabolism that are conserved between yeast and humans. The best-characterized function of La is the binding and protection of Pol III transcripts, such as pre-tRNAs, during their processing. However, La has also been implicated in translational regulation, cancer progression and viral pathogenesis in human cells. La has also been shown to act as an RNA chaperone. Little is known about the mechanisms by which La can carry out these various functions in different cellular compartments. Using yeast as a model organism, we have begun to understand how both human and yeast La traffic between intracellular compartments and how La can bind and differentiate between different RNA targets. Future projects in this area of research will provide further insight into the conserved mechanisms by which this multifunctional protein acts in RNA metabolism and human disease. More recently, our work has expanded into the La-related proteins and how these conserved factors also contribute to gene regulation and challenges to human health.

Students in our group can expect extensive training in techniques used in molecular biology, microbiology and biochemistry. In addition, microbial genetics, cell biology and fluorescence microscopy methods are used.

MarkBayfield

Representative publications:

Porat, J., El Baidouri, M., Grigull, J., Deragon, J.M. and Bayfield, M.A. (2022). The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme.  Nat Commun   13(1):1277

Bayfield, M.A., Vinayak, J., Kerkhofs, K. and Mansouri-Noori, F. (2021).  La proteins couple use of sequence-specific and non-specific binding modes to engage RNA substrates.  RNA Biology 18(2):168-177.

Porat, J., Kothe, U. and Bayfield, M.A. (2021). Revisiting tRNA chaperones: New players in an ancient game. RNA 27(5):543-59

Beenstock, J., Ona, S.M., Porat, J., Orlicky, S., Wan, L.C.K., Ceccarelli, D.F., Maisonneuve, P., Szilard, R.K., Yin, Z., Setiaputra, D., Mao, D.Y.L., Khan, M., Raval, S., Schriemer, D.C., Bayfield, M.A., Durocher, D. and Sicheri, F. (2020). A substrate binding model for the KEOPS tRNA modifying complex. Nat Commun 11(1):6233.

Porat, J. and Bayfield, M.A. (2020). Use of tRNA mediated suppression to assess RNA chaperone function.  Methods Mol Biol  2106:107-120.

Marrella, S.A., Brown, K., Mansouri-Noori, F., Porat, J., Wilson, D.J. and Bayfield, M.A. (2019).  An interdomain bridge influences RNA binding by the human La protein.  J Biol Chem, 294(5):1529-1540

Bayfield, M.A., Kerkhofs, K. and Mansouri-Noori, F. (2019).  C-lection by the DM15 motif gets LARP1 to the TOP.  Structure 27(12):1737-1739

Ehyai, S., Miyake, T., Williams, D., Vinayak, J., Bayfield, M.A. and McDermott, J.C.  (2018) FMRP recruitment of β-catenin to the translation pre-initiation complex represses translation. EMBO Reports, 19(12). pii: e45536. doi: 10.15252/embr.201745536

Vinayak J., Marrella S.A., Hussain R.H., Rozenfeld L., Solomon K., Bayfield M.A. (2018). Human La binds mRNAs through contacts to the poly(A) tail. Nucleic Acids Res 46(8):4228-4240.

Vakiloroayaei, A., Shah, N.S. Oeffinger, M. and Bayfield, M.A. (2017). The RNA chaperone La promotes pre-tRNA maturation via indiscriminate binding of both native and misfolded targets. Nucleic Acids Res 45(19): 11341–11355