Page 27 - Hormel Report 2023

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PUBLICATION HIGHLIGHTS:
• Le, L. T. M., Thompson, J. R., Dehghani-Ghahnaviyeh, S., Pant, S., Dang, P. X., French, J. B., Kanikeyo, T., Tajkhorshid, E., & Alam, A. (2023). Cryo-EM structures of human ABCA7 provide insights into its phospholipid translocation mechanisms. EMBO Journal, 42(3), 14.
• Kim-Holzapfel, D. M., Dey, R., Richardson, B. C., Arachchige, D., Reddy, K., De Vitto,
H., Bhandari, J., & French, J. B. (2023). Human uridine 5’-monophosphate synthase stores metabolic potential in inactive biomolecular condensates. Journal of Biological Chemistry, 299(3), 14.
• Zaman, A., French, J. B., & Carpino, N. (2023). The Sts Proteins: Modulators of Host Immunity. International Journal of Molecular Sciences, 24(10), 8834.
• Richardson, B. C., Shek, R., Van Voorhis, W. C., & French, J. B. (2022). Structure of Klebsiella pneumoniae adenosine monophosphate nucleosidase. Plos One, 17(10), 12.
Structural Dynamics and Mechanisms of BLUF and LOV Photoreceptor Signaling
We are working to understand how signal transduction occurs in a specific class of photoreceptors, called BLUF and LOV photoreceptors. These proteins are becoming increasingly important for the development of optogenetic devices and therapies – optogenetics uses light to control the function of biomolecules. This technology can be used to selectively target treatments to specific sites or specifically control the timing of drug release.
Our Work is Generously Supported by:
The National Institutes of Health: R35GM124898, R01AI141592, and R21AI156238 The National Science Foundation: CAREER MCB1750637, REU CHE2051087
The Hormel Institute and The Eagles Telethon Postdoctoral Fellowship (Nandini)
ORCID iD: https://orcid.org/0000-0002-6762-1309
Mechanisms of assembly of higher order structures: The protein UMP Synthase is involved in making the building blocks for DNA and is an important target for the develop- ment of new cancer treatments. We have identified new ways that this protein assembles into larger, polymeric structures in order to control its activity level in response to changes in metabolism.
Herpesvirus Proteins that Hijack Purine Metabolism
We are conducting structure-function studies on a group of gamma herpesvirus proteins that interact with, and change, the function of the purine metabolic protein called FGAMS. This work is expected to lead to the development of new ways to prevent and or treat herpesvirus infections, several of which cause cancer.