Flores, Maria
Maria is a student in the Biochemistry, Molecular and Structural Biology Graduate Program. She received her B.S degree from Indiana University Bloomington and then came to UCLA where she joined Prof. Jose Rodriguez’s lab. She entered the CMB training program in 2018
Mentor: Dr. Jose Rodriguez
Prion proteins aggregate in cells and are typically associated with neurodegenerative disorders. The narrative that prions are solely disease-causing agents has dominated prion biology literature, but findings implicate them as being essential for cellular memory. Yeast prions are known for their non-Mendelian elements of phenotypic inheritance, relying only on protein based structural changes, challenging the fundamental nucleic-acid dogma of genetics. This mechanism of inheritance for protein-based traits in yeast and fungi creates a fast route to complexity that is reversible. Prion proteins contain a large number of glutamines and asparagines in their N-terminal domain, suggesting the posibility of forming beta-sheet-rich structures. More recently, several groups have found that functional prion-like proteins are conserved in mammals. Prion-like proteins thus serve positive physiological roles in mammals, suggesting that prion disorders are a rare outcome of a normal structural motif.
My research involves using x-ray crystallography, micro-electron diffraction (MicroED) and cryo-electron microscopy (Cryo-EM) to structurally characterize functional human prions. Investigating prions’ reversible structural conformations may enable a more in-depth understanding of the mechanisms that allow such proteins to adopt prion states and return to soluble forms, an ability that pathogenic prions lack.
