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Martin Horvath

Assistant Professor of Biology

B.S. Brown University

Ph.D. University of Chicago

Research

References

horvath@biology.utah.edu

Martin Horvath's Lab Page

Research

Telomeres are special DNA-protein complexes that distinguish natural chromosome ends from broken ends produced by DNA damage. Changes in telomere structure relate to important biological processes like aging and cancer. We would like to know how telomere proteins recognize their DNA binding sites and use both biochemical binding assays and x-ray crystallography to address questions like, What amino acid residues are important for DNA binding affinity and sequence specificity?, How does protein domain architecture and quarternary structure relate to binding cooperativity?, and Why are certain aspects of telomere end structure preserved through evolution?

Cell signaling provides the molecular basis for cell-to-cell communication and allows cells to respond to changes in their environment. In collaboration with Baldomero Olivera, we are using x-ray crystallography to determine the structures of cone snail neurotoxins that interfere with ion channel function. Recent results point to a common origin for one such toxin and protease inhibitors like bovine pancreatic trypsin inhibitor. In another project, we are using a combination of genetics, biochemistry, and x-ray crystallography to determine how a class PP2C protein phosphatase is regulated and targeted to its cognate MAP kinase.

(A) Structure of a telomere end from Oxytricha nova with protein-protein interactions involving alpha and beta subunits highlighted. (B) Fusion proteins designed as new combinations of domains and subunits derived from the native alpha and beta subunits. (C) Telomere DNA binding affinity is linked to cooperative protein-protein interactions retained in the tight-binding p85ab fusion protein (squares) but missing in the p66aNb and p61aNb D fusion proteins (circles).

 

References