Off-campus WSU users: To download campus access dissertations, please use the following link to log into our proxy server with your WSU access ID and password, then click the "Off-campus Download" button below.
Non-WSU users: Please talk to your librarian about requesting this dissertation through interlibrary loan.
Access Type
WSU Access
Date of Award
January 2022
Degree Type
Dissertation
Degree Name
Ph.D.
Department
Biochemistry and Molecular Biology
First Advisor
Bharati Mitra
Abstract
Transition metals are important for maintaining life as they catalyze important enzymatic reactions, provide structural support for proteins, and regulate cellular functions. Despite their importance, transition metals are toxic in excess concentrations. Therefore, their levels need to be regulated. Transport proteins are a critical component of transition metal regulation. The P1-Type ATPase and ZIP family of proteins constitute two important families of transport proteins, which function to regulate transition level metals in both bacteria and humans. ZntA and ZupT are the two functioning proteins from Escherichia coli that represent these two families. Their study can illuminate conserved properties with human homologs. This work focuses on understanding the molecular properties of these two proteins with an emphasis on the metal binding sites in each. It was found that a novel splice variant from ATP7B modeled with ZntA had an altered meta binding stoichiometry, driven by a confirmational change in dimerization. For ZupT, it was found that zinc and iron had distinct metal binding sites and had cooperative transport. The role of manganese transport by ZupT was also examined. Together this work presents lacking biochemical characterization to compliment the extensive cell and animal model knowledge.
Recommended Citation
Roberts, Cameron Sevon, "Investigating The Metal Binding And Transport Properties Of Znta And Zupt" (2022). Wayne State University Dissertations. 3580.
https://digitalcommons.wayne.edu/oa_dissertations/3580