The chaperonin proteins form a ubiquitous family of molecular chaperones and are absolutely required for correct folding or assembly of a subset of proteins in the cell. They are divided into two groups based on phylogeny: Group 1 found in bacteria and eukaryotic-organelles and Group 2 found in eukaryotic-cytoplasma and archaea. The two groups share a significant degree of conservation but differ in structure and mechanism and are believed to have evolved to serve specific client proteins. Using archaeal chaperonin from M. maripaludis (MmCCT) as a representative, we report here for the first time that a Group 2 chaperonin can partially replace the function of a Group 1 chaperonin from E. coli (GroEL). We have also identified and characterized two functional variants of MmCCT that show better GroEL complementation and have utilized them for a preliminary mutational analysis of potential client binding residues of MmCCT. We further demonstrate an initiative using a tagging approach for identification of bacterial proteins that interact with MmCCT in vivo. We suggest that our findings provide a novel platform for genetic dissection of MmCCT using a comparatively simple host, E. coli, which in turn can help identify properties of this archaeal chaperonin and provide insights for structure-function co-relations of Group 2 chaperonins in general.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:600344 |
| Date | January 2014 |
| Creators | Shah, Riddhi |
| Publisher | University of Birmingham |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | http://etheses.bham.ac.uk//id/eprint/4957/ |
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