Orientation of small multidrug resistance transporter subunits in the membrane: correlation with the positive-inside rule

Journal of Molecular Biology
Magdalena A KolbuszJuke S Lolkema

Abstract

Small multidrug resistance (SMR) transport proteins provide a model for the evolution of larger two-domain transport proteins. The orientation in the membrane of 27 proteins from the SMR family was determined using the reporter fusion technique. Nine members were encoded monocistronically (singles) and shown to insert in both orientations (dual topology). Eighteen members were encoded in pairs on the chromosome and shown to insert in fixed orientations; the two proteins in each pair invariably had opposite orientations in the membrane. Interaction between the two proteins in pairs was demonstrated by copurification. The orientation in the membrane of either protein in the pair was affected only marginally by the presence of the other protein. For the proteins in pairs, the orientation in the membrane correlated well with the distribution of positively charges residues (R+K) over the cytoplasmic and extracellular loops (positive-inside rule). In contrast, dual-topology insertion of the singles was predicted less well by the positive-inside rule. Three singles were predicted to insert in a single orientation with the N-terminus and the C-terminus at the extracellular side of the membrane. Analysis of charge distributions suggests...Continue Reading

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Citations

Aug 21, 2012·FEMS Microbiology Letters·Rene Martínez-ValenciaCarlos Cervantes
Jul 13, 2017·Proceedings of the National Academy of Sciences of the United States of America·Nir FlumanGunnar von Heijne
Apr 3, 2019·The Protein Journal·William DowhanMikhail Bogdanov

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