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Understanding the Self-assembly Pathway of Higher Plant Rubisco Activase


Abstract Rubisco activase (Rca) from higher plants is a stromal ATPase essential for reactivating Rubiscos rendered catalytically inactive by endogenous inhibitors. Rca’s functional state is thought to consist of ring-like hexameric assemblies, similar to other members of the AAA+ protein superfamily. However, unlike other members, it does not form obligate hexamers and is quite polydisperse in solution, making elucidation of its self-association pathway challenging. This polydispersity also makes interpretation of traditional biochemical approaches difficult, prompting use of a fluorescence-based technique (Fluorescence Correlation Spectroscopy) to investigate the relationship between quaternary structure and function. Like cotton β Rca, tobacco β ... (more)
Created Date 2018
Contributor Serban, Andrew J (Author) / Wachter, Rebekka M (Advisor) / Levitus, Marcia (Advisor) / Redding, Kevin E (Committee member) / Van Horn, Wade D (Committee member) / Arizona State University (Publisher)
Subject Biochemistry / Activase / ATPase / FCS / Rubisco / Self-assembly / Tobacco
Type Doctoral Dissertation
Extent 230 pages
Language English
Copyright
Note Doctoral Dissertation Biochemistry 2018
Collaborating Institutions Graduate College / ASU Library
Additional Formats MODS / OAI Dublin Core / RIS


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Description Dissertation/Thesis