Double-stranded DNA in cells provides the blueprint for all cellular functions. When it breaks in response to damage inflicted by chemicals, UV radiation, or other factors, cellular DNA-repair machinery jumps into action. But these repair mechanisms are strained when both strands of a molecule of DNA break at the same time.
Learning how those double-stranded breaks are repaired in normal cells and how defects in repair lead to cancer is the goal of a new faculty member in the department of molecular biosciences at the University of Texas at Austin. David Taylor was recruited from the University of California at Berkeley, where he was a postdoctoral fellow, with the help of a CPRIT First-Time Tenure-Track Award from CPRIT. Taylor is the co-director of the Sauer Structural Biology Laboratory.
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Double-stranded DNA in cells provides the blueprint for all cellular functions. When it breaks in response to damage inflicted by chemicals, UV radiation, or other factors, cellular DNA-repair machinery jumps into action. But these repair mechanisms are strained when both strands of a molecule of DNA break at the same time.
Learning how those double-stranded breaks are repaired in normal cells and how defects in repair lead to cancer is the goal of a new faculty member in the department of molecular biosciences at the University of Texas at Austin. David Taylor was recruited from the University of California at Berkeley, where he was a postdoctoral fellow, with the help of a CPRIT First-Time Tenure-Track Award from CPRIT. Taylor is the co-director of the Sauer Structural Biology Laboratory.
As a postdoctoral fellow, he became an expert in using cryo-electron microscopy to image components of cells. Cryo-EM allows for detailed structural information to be obtained from biological molecules. He plans to use his knowledge of cryo-EM to study a protein complex, called MRN, that is crucial for DNA repair.
MRN is a first-responder in cells when DNA damage occurs. But defects in the MRN complex and associated repair pathway are implicated in several cancers, like breast, lung, colon, and skin. Defects in MRN may also play a role in the development of resistance to chemotherapy.
The new Sauer Structural Biology laboratory includes some of the most advanced microscopes in the world to allow scientists to image the MRN complex.
“Cryo-EM has recently become a breakthrough technique because we’ve gotten new equipment that makes it ten times more powerful than it was before,” Taylor says. New detectors enable scientists to create images of complex biological molecules at the atomic level.
“My expertise is in the structural biology of complicated, flexible complexes, and their intermediates,” Taylor says. “And these are paramount in cancer, especially all the proteins that are coming in and out to repair DNA breaks.”
Taylor will collaborate closely with Tanya Paull, a professor in the department of molecular biosciences, who is an expert in the function of cellular proteins. “Combining her expertise in biochemistry with structural information we get from cryo-EM is going to be very powerful,” Taylor says.
Taylor hopes that better understanding how cancer arises can help researchers develop better therapies.
So far, the laboratory is just getting started. But Taylor is already envisioning collaborations with colleagues at the newly opened Dell Medical School. Insights from clinicians can guide him in choosing targets for imaging, like proteins that are important cancer signaling molecules.
Taylor received his undergraduate degree in biochemistry from Syracuse University, and his master’s and Ph.D. in molecular biophysics and biochemistry from Yale University. He became a postdoctoral fellow at Berkeley in 2014.
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