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

doi:10.1007/s12275-012-1326-z

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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; Journal of Microbiology 2012;50(2):256-262.
DOI: https://doi.org/10.1007/s12275-012-1326-z
Published online: April 27, 2012

Department of Microbiology & Molecular Biology, College of Bioscience and Biotechnology, Chungnam National University, Daejeon 305-764, Republic of Korea

Corresponding author: Hee-Moon Park , Tel: +82-42-821-6417,

Received: 30 June 2011 • Accepted: 14 November 2011

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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.

Keywords: α-COP;mutagenesis;Saccharomyces cerevisiae;WD40 domain;yeast two-hybrid

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Effects of Mutations in the WD40 Domain of α-COP on Its Interaction with the COPI Coatomer in Saccharomyces cerevisiae

J. Microbiol. 2012;50(2):256-262. Published online April 27, 2012

DOI: https://doi.org/10.1007/s12275-012-1326-z

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