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Identification Of Novel Interactors Of Sec6 Via Genetic Suppressor Screen Using A Saccharomyces Cerevisiae Genomic Dna Library, Y. Ellen France Phd, Emily Parrish, Raira Ank, Tristan Peterman, Sarah Mork, Billie Mills, Lindsey Duke, Jyoti Lama Apr 2017

Identification Of Novel Interactors Of Sec6 Via Genetic Suppressor Screen Using A Saccharomyces Cerevisiae Genomic Dna Library, Y. Ellen France Phd, Emily Parrish, Raira Ank, Tristan Peterman, Sarah Mork, Billie Mills, Lindsey Duke, Jyoti Lama

Georgia College Student Research Events

Polarized protein secretion is a fundamental process for all organisms, from yeast to higher eukaryotes. The secretory pathway in eukaryotes includes many steps mediated by hundreds of essential proteins. Our interest lies on Sec6, which is an 88kDa protein subunit of the tethering complex named exocyst, which is known to play diverse roles in recognition, tethering, and SNARE-mediated fusion of secretory vesicles. Previous work on Sec6 done by Munson and Songer (2009) explored phenotypes of two novel SEC6 mutant proteins, whose conserved surface amino acids had been altered. Both sec6-49 and sec6-54 mutant alleles displayed severe temperature sensitive growth and ...