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• W23714381 abstract "Research Article1 December 1991free access Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP binding cassette (ABC) protein superfamily. C. Berkower C. Berkower Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author S. Michaelis S. Michaelis Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author C. Berkower C. Berkower Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author S. Michaelis S. Michaelis Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author Author Information C. Berkower1 and S. Michaelis1 1Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205. The EMBO Journal (1991)10:3777-3785https://doi.org/10.1002/j.1460-2075.1991.tb04947.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info STE6, the yeast a-factor transporter, is a member of the ATP binding cassette protein superfamily, which also includes the mammalian multidrug resistance protein and the cystic fibrosis gene product. These proteins contain two homologous halves, each with six membrane spanning segments and a predicted ATP nucleotide binding domain. To assess the importance of the two halves of STE6, and to examine the functional significance of residues conserved among members of the ATP binding cassette superfamily, we introduced mutations into the nucleotide binding domains of STE6. Our analysis demonstrates that both halves of STE6 are critical for function and that some, but not all, mutations analogous to those known to result in cystic fibrosis impair STE6 activity. To examine further the functional contribution of each half of the STE6 protein, we severed the STE6 coding sequence and expressed the two halves of the transporter as separate polypeptides. Whereas ‘half-molecules’ are unable to provide transport function individually, co-expression of both half-molecules in the same cell leads to functional reconstitution of STE6-mediated a-factor transport. Previous ArticleNext Article Volume 10Issue 121 December 1991In this issue RelatedDetailsLoading ..." @default.
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• W23714381 date "1991-12-01" @default.
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• W23714381 title "Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP binding cassette (ABC) protein superfamily." @default.
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• W23714381 doi "https://doi.org/10.1002/j.1460-2075.1991.tb04947.x" @default.
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