Journal of Microbiology

Research Support, Non-U.S. Gov't

Effects of Mutations in the WD40 Domain of α-COP on Its Interaction with the COPI Coatomer in Saccharomyces cerevisiae: Ki-Hyun Kim , Eun Kyung Kim , Ki Young Jeong , Yun-Hee Park , Hee-Moon Park; J. Microbiol. 2012;50(2):256-262. Published online April 27, 2012; DOI: https://doi.org/10.1007/s12275-012-1326-z

Abstract: Replacement of glycine 227 in the fifth WD40 motif of α-COP/Ret1p/Soo1p by charged or aromatic amino acids is responsible for the temperature-dependent osmo-sensitivity of Saccharomyces cerevisiae, while truncations of WD40 motifs exerted a reduction in cell growth rate and impairment in assembly of cell-wall associated proteins such as enolase and Gas1p. Yeast two-hybrid analysis revealed that the ret1-1/soo1-1 mutation of α-COP abolished the interaction with β- and ε-COP, respectively, and that the interaction between α-COP and β-COP relied on the WD40 domain of α-COP. Furthermore, although the WD40 domain is dispensable for interaction of α-COP with ε-COP, structural alterations in the WD40 domain could impair the interaction.

Search