title: Effects of mutations in the WD40 domain of α-COP on its interaction with the COPI coatomer in Saccharomyces cerevisiae.
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 ɛ-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 ɛ-COP, structural alterations in the WD40 domain could impair the interaction.
authors.affiliation: Department of Microbiology & Molecular Biology, College of Bioscience and Biotechnology, Chungnam National University, Daejeon, 305-764, Republic of Korea.
authors.forename: Ki-Hyun
authors.initials: KH
authors.lastname: Kim
authors.forename: Eun Kyung
authors.initials: EK
authors.lastname: Kim
authors.forename: Ki Young
authors.initials: KY
authors.lastname: Jeong
authors.forename: Yun-Hee
authors.initials: YH
authors.lastname: Park
authors.forename: Hee-Moon
authors.initials: HM
authors.lastname: Park
mesh_terms: D020755:Coat Protein Complex I / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020756:Coatomer Protein / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D011485:Protein Binding; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D020755:Coat Protein Complex I; D020756:Coatomer Protein; D029701:Saccharomyces cerevisiae Proteins