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Investigating the interactions that govern the architecture of the carboxysomal shell

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dc.contributor.advisor Kimber, Matthew
dc.contributor.author Samborska, Bozena
dc.date.accessioned 2021-04-19T14:27:02Z
dc.date.available 2021-04-19T14:27:02Z
dc.date.copyright 2010
dc.identifier.uri https://hdl.handle.net/10214/24985
dc.description.abstract Photosynthetic cyanobacteria optimize carbon fixation by enhancing the enzymatic activity of Rubisco through its co-encapsulation with carbonic anhydrase (CA) in proteinaceous organelle-like microcompartments called carboxysomes. Carboxysomes are large icosahedral particles that are composed of a thin outer protein shell, consisting exclusively of thousands of protein copies that collectively form this shell. The major components, CcmK1, CcmK2, and CcmK4, form hexagonal hexamers and further tile into a gapless sheet to form the facets of the shell, while pentameric CcmL occupies the vertices. To date, the interactions between the shell proteins have not been investigated biochemically. A FRET based method was developed to investigate interactions governing carboxysomal shell architecture. The shell proteins (CcmK(1,2,4)) interact interchangeably with one another, as well as with CcmL. Furthermore, CcmK2 assembles as a distinct dodecamer, and is proposed to form a double-layered shell subdomain. Additionally, the sidedness of the shell is investigated from shell-interior interaction data.
dc.language.iso en
dc.subject carboxysomal shell
dc.subject architecture
dc.subject carbonic anhydrase
dc.subject carboxysomes
dc.subject shell-interior interaction
dc.title Investigating the interactions that govern the architecture of the carboxysomal shell
dc.type Thesis
dc.degree.name Master of Science
dc.degree.department Department of Molecular and Cellular Biology
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