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• W201895147 abstract "Research Article1 August 1995free access Membrane insertion and assembly of ductin: a polytopic channel with dual orientations. J. Dunlop J. Dunlop CRC Beatson Laboratories, Beatson Institute for Cancer Research, Bearsden, Glasgow, UK. Search for more papers by this author P. C. Jones P. C. Jones CRC Beatson Laboratories, Beatson Institute for Cancer Research, Bearsden, Glasgow, UK. Search for more papers by this author M. E. Finbow M. E. Finbow CRC Beatson Laboratories, Beatson Institute for Cancer Research, Bearsden, Glasgow, UK. Search for more papers by this author J. Dunlop J. Dunlop CRC Beatson Laboratories, Beatson Institute for Cancer Research, Bearsden, Glasgow, UK. Search for more papers by this author P. C. Jones P. C. Jones CRC Beatson Laboratories, Beatson Institute for Cancer Research, Bearsden, Glasgow, UK. Search for more papers by this author M. E. Finbow M. E. Finbow CRC Beatson Laboratories, Beatson Institute for Cancer Research, Bearsden, Glasgow, UK. Search for more papers by this author Author Information J. Dunlop1, P. C. Jones1 and M. E. Finbow1 1CRC Beatson Laboratories, Beatson Institute for Cancer Research, Bearsden, Glasgow, UK. The EMBO Journal (1995)14:3609-3616https://doi.org/10.1002/j.1460-2075.1995.tb00030.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Ductin is a highly conserved and polytopic transmembrane protein which is the subunit c component of the vacuolar H(+)-ATPase (V-ATPase) and a component of a connexon channel of gap junctions. Previous studies have suggested that ductin in the V-ATPase has the opposite orientation of ductin in a connexon. Using an in vitro translation system coupled to microsomes derived from the endoplasmic reticulum, we show that ductin is co-translationally inserted into the membrane bilayer, suggesting a dependency on the signal recognition particle for synthesis. By attaching a C-terminal polypeptide derived from beta-lactamase and by using cysteine replacement coupled to chemical labelling, we show that ductin is inserted into the microsomal membrane in both orientations in similar proportions. In contrast, squid rhodopsin appears to be inserted in a single orientation. Changing conserved charged residues at the N-terminus of ductin does not affect the ratio of the two orientations. Once in the microsomal membrane, ductin assembles into an oligomeric complex which contains a pore accessible to a water-soluble probe, reminiscent of the ductin complex found in the V-ATPase and a connexon. Previous ArticleNext Article Volume 14Issue 151 August 1995In this issue RelatedDetailsLoading ..." @default.
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• W201895147 title "Membrane insertion and assembly of ductin: a polytopic channel with dual orientations." @default.
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