The Power of Pichia
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Location
Biology Building, Room 101
Start Date
3-10-2019 6:00 PM
End Date
3-10-2019 7:00 PM
Description
Heterologous protein expression consists of engineering an organism to express a protein which it does not produce in nature, such as human insulin made by a microbe. The methylotrophic yeast Pichia pastoris has been a popular host for heterologous protein expression in order to produce thousands of recombinant protein products for research, clinical, and industrial purposes. Because this yeast secretes very few of its own proteins, the exported recombinant protein is the major polypeptide in the extracellular medium, making purification relatively easy. Unfortunately, a disadvantage to programmed export is that some recombinant proteins intended for secretion are retained within in the cell and may be subsequently degraded. A mutant strain isolated in our lab, containing a disruption of the BGS13 gene, has displayed elevated levels of secretion for a variety of reported proteins. Therefore, we are trying to understand how mutation of this BGS13 gene leads to an abnormal Bgs13 protein which in turn results in improved secretion of many different recombinant proteins. Our long term goal is to apply this understanding of the BGS13 gene to create new versions of Pichia pastoris expression strains that will be able to secrete larger amounts of valuable recombinant proteins.
The Power of Pichia
Biology Building, Room 101
Heterologous protein expression consists of engineering an organism to express a protein which it does not produce in nature, such as human insulin made by a microbe. The methylotrophic yeast Pichia pastoris has been a popular host for heterologous protein expression in order to produce thousands of recombinant protein products for research, clinical, and industrial purposes. Because this yeast secretes very few of its own proteins, the exported recombinant protein is the major polypeptide in the extracellular medium, making purification relatively easy. Unfortunately, a disadvantage to programmed export is that some recombinant proteins intended for secretion are retained within in the cell and may be subsequently degraded. A mutant strain isolated in our lab, containing a disruption of the BGS13 gene, has displayed elevated levels of secretion for a variety of reported proteins. Therefore, we are trying to understand how mutation of this BGS13 gene leads to an abnormal Bgs13 protein which in turn results in improved secretion of many different recombinant proteins. Our long term goal is to apply this understanding of the BGS13 gene to create new versions of Pichia pastoris expression strains that will be able to secrete larger amounts of valuable recombinant proteins.
Speaker Bio
Both Joan and Geoff Lin-Cereghino earned their Ph.D. in biology from the University of California, San Diego after doing undergraduate degrees in molecular biology at Princeton and biochemistry at University of California, Davis, re-spectively. Both taught at Haverford College as visiting professors in the biology department for a year and then moved to Oregon. At the Oregon Graduate Institute (now part of the Oregon Health and Sciences University) both Joan and Geoff ended up doing postdoctoral research on the methylotrophic yeast Pichia pastoris under the direction of Dr. Jim Cregg. Joan and Geoff came to Pacific twenty years ago in a joint position as ¾ of a professor each. They still share an office, a lab, two kids (Ted ’19 and Grace), and a chicken named Gloria.