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KMID : 0880220120500020256
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Journal of Microbiology
2012 Volume.50 No. 2 p.256 ~ p.262
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Effects of mutations in the WD40 domain of α-COP on its interaction with the COPI coatomer in Saccharomyces cerevisiae
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Kim Ki-Hyun
Kim Eun-Kyung
Jeong Ki-Young
Park Yun-Hee
Park Hee-Moon
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Abstract
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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 ?-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 ?-COP, structural alterations in the WD40 domain could impair the interaction.
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KEYWORD
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α-COP, mutagenesis, Saccharomyces cerevisiae, WD40 domain, yeast two-hybrid
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