A cell fusion protein in yeast interacts with proteins required for mating and polarized growth
Year: 1997
Type: dissertation
Abstract: Saccharomyces cereuisiae provides an elegant model for the study ' of cell conjugation'and fusion.Fuslp is required for efficient cell fusion \ during the mating process, and localizes to the cell surface.It is strongly induced in response to pher~mone, possesses a single transmembrane domain, iS 0-glycosylated, and contains one SH3 (src-homology' three).domain at the C-terminus of its cytoplasmic portion.In this study I \ 10 adopted the two-hybrid system to test Fuslp for interaction with various proteins involved in cell fusion and signalling.Fuslp interacted with Rvs167p, a cytoskeletal associated protein, Fus2p, a second pheromone inducible and fusion related protein, Fus3p, Ksslp, Stellp, SteSp, and Ste7p, components of the MAPK pheromone response pathway, and ChsSp, a protein that is potentially involved in vesicular transport.I also screened two-hybrid libraries with the cytoplasmic portion of Fuslp, including the SH3 domain.I isolated Bud2p, the GTPase activating protein for Rsrlp, Bnrlp, a formin homolog, and Yn1075wp, Yn1054wp, and Ylrll7cp, three previously unidentified ORF encoded proteins.Further two-hybrid experiments demonstrated that Bnrlp interacts with Axllp, a protein responsible for the haploid specific axial budding pattern. 1 term the complex of Fuslp and aforementioned proteins a "fusion complex".1 propose that the "fusion complex" links the pheromone response pathway to proteins that participate in both reorganization of the 5-' \.actin cytoskeleton and endocytotic vesicular recycling., .
Author: Steven John Ritchie
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W183870177