Title

Can potential mutant strains of the BGS13 gene lead to supersecretion of Pichia pastoris?

Poster Number

13B

Lead Author Major

Biological Sciences

Lead Author Status

Senior

Second Author Major

Pre-Dentistry

Second Author Status

Junior

Format

Poster Presentation

Faculty Mentor Name

Geoffrey Lin-Cereghino

Faculty Mentor Email

glincere@pacific.edu

Faculty Mentor Department

Biological Sciences

Abstract/Artist Statement

Pichia pastoris is a yeast used for expressing recombinant proteins and products such as antibiotics. Pichia pastoris is good at secreting certain proteins which is crucial because secreted proteins are easier to purify than intracellular peptides. Our lab has previously isolated a mutant strain of the BGS13 gene that is known to be a supersecretor. This strain is able to secrete elevated levels of B-galactosidase and other reporter proteins. The BGS13 gene encodes a kinase that is believed to be involved in cell wall integrity. Our goal is to see if BGS13 mutants with different localization or protein kinase C (PKC) activity lead to a supersecretion. We used site-directed mutagenesis to generate two new versions of the BGS13 protein and analyzed the effects of the mutations on their localization using fluorescence microscopy and and on their PKC activity using an ELISA based assay. Our results can be used in future experiments to create strains with increased secretion of different proteins.

Location

DeRosa University Center Ballroom

Start Date

27-4-2018 10:00 AM

End Date

27-4-2018 12:00 PM

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Apr 27th, 10:00 AM Apr 27th, 12:00 PM

Can potential mutant strains of the BGS13 gene lead to supersecretion of Pichia pastoris?

DeRosa University Center Ballroom

Pichia pastoris is a yeast used for expressing recombinant proteins and products such as antibiotics. Pichia pastoris is good at secreting certain proteins which is crucial because secreted proteins are easier to purify than intracellular peptides. Our lab has previously isolated a mutant strain of the BGS13 gene that is known to be a supersecretor. This strain is able to secrete elevated levels of B-galactosidase and other reporter proteins. The BGS13 gene encodes a kinase that is believed to be involved in cell wall integrity. Our goal is to see if BGS13 mutants with different localization or protein kinase C (PKC) activity lead to a supersecretion. We used site-directed mutagenesis to generate two new versions of the BGS13 protein and analyzed the effects of the mutations on their localization using fluorescence microscopy and and on their PKC activity using an ELISA based assay. Our results can be used in future experiments to create strains with increased secretion of different proteins.