The AAA+ ATPase ClpC-M Domain is a Secondary Interaction Site For the Sporulation-Specific Adaptor Protein MdfA in the Bacterium Bacillus Subtilis
dc.contributor.advisor | Amy, Camp | |
dc.contributor.author | Morrison, Jade | |
dc.date.accessioned | 2025-07-15T14:02:37Z | |
dc.date.available | 2025-07-15T14:02:37Z | |
dc.date.gradyear | 2025 | |
dc.description.abstract | Protein degradation is a tightly regulated mechanism in bacterial cells that ensures that the correct proteins are being degraded appropriately to avoid harmful consequences within the cell. ClpCP is an example of an AAA+ protease that facilitates proteolysis within bacterial cells through a degron tag or with the assistance of an adaptor protein. MdfA is a recently discovered sporulation-specific adaptor protein that interacts with ClpCP within the bacterium, Bacillus subtilis. Based on results from a previous study, it is speculated that MdfA interacts with the ClpC-M domain, corresponding with an AlphaFold Multimer structure that collaborators constructed. This study investigates whether the ClpC M-domain is a site of interaction for MdfA, which was tested by mutating the appropriate codon of residues located at the contact point between the M-domain and MdfA C-terminal domain. A series of bacterial two-hybrid assays has demonstrated that the M-domain is a potential interaction site and that the ClpC M-domain residues are more critical for MdfA than MecA. The results and a parallel study by a Camp lab member, Jen Butler, support the hypothesis that the M-domain is a secondary interaction site for MdfA. | |
dc.description.sponsorship | Biological Sciences | |
dc.identifier.uri | https://hdl.handle.net/10166/6774 | |
dc.language.iso | en_US | |
dc.rights.restricted | restricted | |
dc.subject | Molecular Biology | |
dc.title | The AAA+ ATPase ClpC-M Domain is a Secondary Interaction Site For the Sporulation-Specific Adaptor Protein MdfA in the Bacterium Bacillus Subtilis | |
dc.type | Thesis | |
mhc.degree | Undergraduate | |
mhc.institution | Mount Holyoke College |