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• W1209714687 abstract "Research Article15 September 1994free access Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis. J.R. Lamb J.R. Lamb Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. Search for more papers by this author W.A. Michaud W.A. Michaud Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. Search for more papers by this author R.S. Sikorski R.S. Sikorski Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. Search for more papers by this author P.A. Hieter P.A. Hieter Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. Search for more papers by this author J.R. Lamb J.R. Lamb Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. Search for more papers by this author W.A. Michaud W.A. Michaud Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. Search for more papers by this author R.S. Sikorski R.S. Sikorski Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. Search for more papers by this author P.A. Hieter P.A. Hieter Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. Search for more papers by this author Author Information J.R. Lamb1, W.A. Michaud1, R.S. Sikorski1 and P.A. Hieter1 1Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. The EMBO Journal (1994)13:4321-4328https://doi.org/10.1002/j.1460-2075.1994.tb06752.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Cdc16p, Cdc23p and Cdc27p are all essential proteins required for cell cycle progression through mitosis in Saccharomyces cerevisiae. All three proteins contain multiple tandemly repeated 34 amino acid tetratricopeptide repeats (TPRs). Using two independent assays, two-hybrid analysis in vivo and co-immunoprecipitation in vitro, we demonstrate that Cdc16p, Cdc23p and Cdc27p self associate and interact with one another to form a macromolecular complex. A temperature sensitive mutation in the most highly conserved TPR domain of Cdc27p results in a greatly reduced ability to interact with Cdc23p, but has no effect on interactions with wild-type Cdc27p or Cdc16p. The specificity of this effect indicates that TPRs can mediate protein-protein interactions and that this mutation may define an essential interaction for cell cycle progression in yeast. The conservation of at least two of the three proteins from yeast to man suggests that this protein complex is essential for mitosis in a wide range of eukaryotes. Previous ArticleNext Article Volume 13Issue 181 September 1994In this issue RelatedDetailsLoading ..." @default.
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