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Wittrup, K. Dane Bannister, Sarah Jane 2015-09-25T20:44:17Z 2015-09-25T20:44:17Z 10000-01-01 2000 2000 The work described in this thesis involves the effect of cellular redox factors on BPTI secretion. Glutathione levels and redox state were altered in an attempt to determine if optimal BPTI secretion requires a certain total glutathione level and/or redox state. Evidence for an optimal glutathione level that results in high BPTI secretion was obtained. Thioredoxin deficiency was also shown to increase BPTI secretion. Several possible actors in the ER oxidative protein folding chain were identified and their effects on BPTI secretion measured. Overexpression of Ero1p was shown to increase BPTI secretion, while overexpression of flavin-containing monooxygenase (FMO) and Fun9p did not. Overexpression of two potential sulfhydryl oxidases, Erv1p and Erv2p, did not increase BPTI secretion. The addition of ubiquinone, which has been shown to be an electron acceptor from the E. coli disulfide bond formation chain, increased BPTI secretion from cultures overexpressing FMO, but under no other scenarios. A system has been set up to utilize the yeast surface display system to screen a cDNA library for factors that increase BPTI surface display, and therefore secretion. The information gathered in this work identifies new directions for increasing protein secretion in yeast. Made available in DSpace on 2015-09-25T20:44:17Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9989939.pdf: 5248570 bytes, checksum: 59edda116c9a78a69f86e2dfe430edd1 (MD5) Previous issue date: 2000 Embargo set by: Seth Robbins for item 83760 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 126 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000. http://hdl.handle.net/2142/82479 (MiAaPQ)AAI9989939 eng Biology, Microbiology Increasing Heterologous Protein Secretion From the Yeast S. Cerevisiae Through Manipulation of Cellular Redox Factors text Chemical Engineering Chemical Engineering University of Illinois at Urbana-Champaign Dissertation Ph.D.