A molecular investigation of the interaction between Rubisco and beta-carboxysome interior organizer CcmM

dc.contributor.advisorKimber, Matthew
dc.contributor.authorRyan, Patrick
dc.date.accessioned2017-12-22T18:20:54Z
dc.date.available2017-12-22T18:20:54Z
dc.date.copyright2017-10
dc.date.created2017-12-20
dc.date.issued2017-12-22
dc.degree.departmentDepartment of Molecular and Cellular Biologyen_US
dc.degree.grantorUniversity of Guelphen_US
dc.degree.nameMaster of Scienceen_US
dc.degree.programmeMolecular and Cellular Biologyen_US
dc.description.abstractCyanobacteria and some chemoautotrophs sequester Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in close proximity to CO2 using large proteinaceous microcompartments called carboxysomes, to improve carbon fixation efficiency. Carboxysomes are built from tens of thousands of protein subunits with a closed icosahedral shell that is selectively permeable for certain substrates and metabolites. This shell encases functional enzymes, including Rubisco, within. CcmM is an interior β-carboxysome protein that has been implicated in organizing the carboxysome interior. The C-terminal domain of CcmM is built of three to five subunits that closely resemble the small subunit of Rubisco, and have been implicated in organizing Rubisco into a core that the carboxysomal shell forms around. This thesis reports the first known X-ray crystallographic structure of the first C-terminal domain in the chain “SS1” from T. elongatus BP-1. Förster Resonance Energy Transfer, Surface Plasmon Resonance and Native mass spectrometry experiments show CcmM binds Rubisco with micromolar affinities. Six SS1 domains can bind to Rubisco with no indication of RbcS release, suggesting that binding does not fully displace RbcS. A novel molecular binding model for the CcmM-Rubisco complex is proposed.en_US
dc.description.sponsorshipNatural Sciences and Engineering Research Council of Canada
dc.identifier.urihttp://hdl.handle.net/10214/12120
dc.language.isoenen_US
dc.publisherUniversity of Guelphen_US
dc.rights.licenseAll items in the Atrium are protected by copyright with all rights reserved unless otherwise indicated.
dc.subjectcarboxysomeen_US
dc.subjectrubiscoen_US
dc.subjectccmmen_US
dc.titleA molecular investigation of the interaction between Rubisco and beta-carboxysome interior organizer CcmMen_US
dc.typeThesisen_US

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