Poster Title
P-40 Carboxypeptidase folding mechanisms in the absence of a chaperone-like prodomain
Abstract
Most carboxypeptidases contain a second domain that functions as an intramolecular chaperone to aid in protein folding. Carboxypeptidase O (CPO), however, is composed of only an enzymatic domain with a short N-terminal extension and a C-terminal signal peptide necessary for membrane attachment via a GPI anchor. To investigate the role of these segments in folding, site-directed mutagenesis was performed. Mutants lacking the GPI signal peptide were expressed at lower levels in HEK293T cells, suggesting a function of this segment as intramolecular chaperone. In order to confirm this role, expression was performed in Sf9 insect cells. Purification and characterization of CPO mutants is ongoing.
Location
Buller Hallway
Start Date
3-6-2015 2:30 PM
End Date
3-6-2015 4:00 PM
P-40 Carboxypeptidase folding mechanisms in the absence of a chaperone-like prodomain
Buller Hallway
Most carboxypeptidases contain a second domain that functions as an intramolecular chaperone to aid in protein folding. Carboxypeptidase O (CPO), however, is composed of only an enzymatic domain with a short N-terminal extension and a C-terminal signal peptide necessary for membrane attachment via a GPI anchor. To investigate the role of these segments in folding, site-directed mutagenesis was performed. Mutants lacking the GPI signal peptide were expressed at lower levels in HEK293T cells, suggesting a function of this segment as intramolecular chaperone. In order to confirm this role, expression was performed in Sf9 insect cells. Purification and characterization of CPO mutants is ongoing.
Acknowledgments
Undergraduate Research Scholar
Advisor: Peter Lyons, Biology