Abstract
Auxin is a major plant hormones regulating plant growth and development. The direction of auxin transport is based on the non-uniform distribution of auxin carriers on the plasma membrane. However, auxin carriers play an important role in plant physiology. The auxin influx is actively mediated by the AUX1 and LAX family of transmembrane proteins. The amino acids of AUX1 are composed of 485 residues and the molecular weight of AUX1 is about 54 kDa. In this work, the Arabidopsis AUX1 with a C-terminal His6 was constructed into pREP41 vector. AUX1 was accordingly heterologously expressed in fission yeast, Schizosaccharomyces pombe (HM123). With the highest yield of AUX1, we used the detergent FC-12 (Foscholine-12) to solubilize AUX1 from membranes. Furthermore, both cation exchanger and the metal chelating affinity chromatography were sequentially used to purify AUX1. The prepared AUX1 is expected to grow crystals for structure analysis in future.