Title |
Effects of Mutations in the WD40 Domain of α-COP on Its Interaction with the COPI Coatomer in Saccharomyces cerevisiae |
Author |
Ki-Hyun Kim, Eun Kyung Kim, Ki Young Jeong, Yun-Hee Park, and Hee-Moon Park* |
Address |
Department of Microbiology & Molecular Biology, College of Bioscience and Biotechnology, Chungnam National University, Daejeon 305-764, Republic of Korea |
Bibliography |
Journal of Microbiology, 50(2),256-262, 2012,
|
DOI |
|
Key Words |
α-COP, mutagenesis, Saccharomyces cerevisiae, WD40 domain, yeast two-hybrid |
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. |