BMSB graduate students Janine Fu, Calina Glynn, and Jiahui Lu have been selected as 2020-21 Audree Fowler Fellows in Protein Science.
Each Fellow will present a talk at the Audree V. Fowler Fellowships in Protein Science Special Seminar on Tuesday, October 6, 2020 from 12:00 pm to 1:00 p.m. Click here for Zoom details.
In 2008, an endowment from UCLA Chemistry & Biochemistry alumna Dr. Audree Fowler (B.S. ’56, Ph.D. ’63) established the Audree Fowler Fellows in Protein Science. Applications are solicited from graduate students in the Molecular Biology Interdepartmental (MBI) Ph.D. Program, Biological Chemistry, and Chemistry & Biochemistry Departments. Three recipients are presented with awards of $5,000 each and, when there is not a pandemic; present their research at the Annual MBI Retreat. "The sciences gave me a great life. Now I want to help others have access to the same opportunities I enjoyed," Fowler explained when she established the endowment.
About the 2020-21 Audree Fowler Fellows in Protein Science
Janine Fu is a fourth year Biochemistry, Molecular, and Structural Biology (BMSB) student in Professor Joseph Loo’s group. She received her B.S. in Biochemistry at UCLA and worked in Professor Robert Clubb’s lab, studying the molecular basis of Gram-positive bacterial surface display machinery using structural and biochemical techniques.
Janine’s graduate research focuses on proteomics and understanding the role post-translational modifications play in bacterial systems. Protein acylation, which is known to affect enzymatic activity, can occur spontaneously from elevated metabolite intermediates and modification levels fluctuate with metabolic flux. Her research studies how protein acylation can act as a mechanism of metabolic regulation. Janine utilizes mass spectrometry to investigate the proteomes of different cellular metabolic states and to characterize their protein acylation profiles. Her work also aims to understand the regulation of these modifications and their physiological effects.
The title of Janine’s Fowler Fellow talk is “Proteome-wide investigation of protein acylation in the metabolically versatile Rhodopseudomonas palustris”.
Calina Glynn (Callie) is a fifth year Biochemistry, Molecular and Structural Biology (BMSB) student in Professor Jose Rodriguez’s group. Prior to coming to UCLA in 2016, Callie received her B.A. in Biochemistry and Molecular Biology from Boston University, where she studied Fe-S cluster binding proteins with Dr. Deborah Perlstein.
Callie’s graduate work focuses on uncovering the structures of prion fibrils that bestow them with unique biophysical properties. Prion diseases arise via the self-templated misfolding of the soluble prion protein into pathogenic protease, denaturant, and heat resistant prion fibrils (PrPSc). Callie has uncovered the structure of a protease and denaturant-resistant human prion fibril that explains the unique biophysical properties characteristic of PrPSc using cryo-electron microscopy. Callie aims to uncover differences in the favored fold, stability, and seeding ability of fibrils from disease-associated variants of the human prion protein and other mammalian prion proteins whose aggregation leads to disease.
The title of Callie’s Fowler Fellow talk is “Structures at the Core of Mammalian Prions”.
Jiahui Lu is a fourth year Biochemistry, Molecular and Structural Biology (BMSB) graduate student in Professor David Eisenberg’s group. As an undergraduate at UC Davis, Jiahui worked on biochemical and structural studies of proteins involved in Tuberculosis assimilation pathways, and received her B.S. degree in the summer of 2017.
Jiahui’s graduate research studies the ribonucleoprotein heterogeneous nuclear ribonucleoprotein A2 (hnRNPA2). It functions in RNA metabolism and is associated with cellular membraneless organelles. The low-complexity domain (LCD) of hnRNPA2 can liquid-liquid phase separate and form a hydrogel in vitro where fibril networks are found. Cellular stress and mutations can lead to fibril formation and thus neurodegenerative diseases such as Multisystem Proteinopathy (MSP). Jiahui applies biochemical and structural studies, using cryo-electron microscopy and crystallography, to understand how the reversible, functional fibrils formed by the LCD of hnRNPA2 can convert to pathogenic fibrils, leading to neurodegenerative diseases.
The title of Jiahui’s Fowler Fellow talk is “CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid”.
Penny Jennings, UCLA Department of Chemistry & Biochemistry, firstname.lastname@example.org. Photos and biographies courtesy of the Molecular Biology Institute.