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. 2015 Feb 10;6:47. doi: 10.3389/fpls.2015.00047

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Copyright © 2015 Safiarian, Pertl-Obermeyer, Lughofer, Hude, Bertl and Obermeyer.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Co-sedimentation of LilKT1 with yeast organelle markers. (A) Distribution of membrane protein and sucrose concentration in a continuous sucrose gradient collected after 16 h centrifugation (n = 5 ± S.D.) (B) Typical pattern of membrane proteins along the sucrose gradient. 30 μl of sucrose-adjusted fraction loaded per lane. (C) Typical distribution of plasma membrane (Pma1p), ER (Dpm1p), and vacuole (Vma1p) marker enzymes in the sucrose gradient. (D) Plasma membrane fractions (3–8) of three gradients were pooled, proteins were precipitated and transferred to NC membranes after SDS-PAGE. The proteins AKT1, Pma1p and the HA-tag of LilKT1 were detected with respective antibodies in the pooled fractions of PM fractions (underlined) of PLY240 yeast mutants expressing AKT1 or LilKT1 alone and the combination of AKT1 and LilKT1 (n.d., not determined).