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Plant Cell Advance Online Publication
Published on October 14, 2004; 10.1105/tpc.104.024737

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Received June 4, 2004
Accepted August 22, 2004

Structure-Function Analysis of the Presumptive Arabidopsis Auxin Permease AUX1

Ranjan Swarup 1, Joanna Kargul 1, Alan Marchant 1, Daniel Zadik 1, Abidur Rahman 2, Rebecca Mills 3, Anthony Yemm 4, Sean May 1, Lorraine Williams 3, Paul Millner 5, Seiji Tsurumi 2, Ian Moore 6, Richard Napier 7, Ian D. Kerr 8, and Malcolm J. Bennett 1*

1 School of Biosciences, Sutton Bonington Campus, University of Nottingham, United Kingdom
2 Centre for Support to Research and Education Activities Isotope Division, Kobe University, Kobe, Japan
3 School of Biological Sciences, University of Southampton, United Kingdom
4 School of Biosciences, Sutton Bonington Campus, University of Nottingham, United Kingdom; Warwick-HRI, University of Warwick, Wellesbourne, United Kingdom
5 School of Biochemistry and Molecular Biology, University of Leeds, Leeds, United Kingdom
6 Plant Sciences, University of Oxford, United Kingdom
7 Warwick-HRI, University of Warwick, Wellesbourne, United Kingdom
8 School of Biomedical Sciences, Queens Medical Centre, University of Nottingham, United Kingdom

* To whom correspondence should be addressed. E-mail: malcolm.bennett{at}nottingham.ac.uk.

We have investigated the subcellular localization, the domain topology, and the amino acid residues that are critical for the function of the presumptive Arabidopsis thaliana auxin influx carrier AUX1. Biochemical fractionation experiments and confocal studies using an N-terminal yellow fluorescent protein (YFP) fusion observed that AUX1 colocalized with plasma membrane (PM) markers. Because of its PM localization, we were able to take advantage of the steep pH gradient that exists across the plant cell PM to investigate AUX1 topology using YFP as a pH-sensitive probe. The YFP-coding sequence was inserted in selected AUX1 hydrophilic loops to orient surface domains on either apoplastic or cytoplasmic faces of the PM based on the absence or presence of YFP fluorescence, respectively. We were able to demonstrate in conjunction with helix prediction programs that AUX1 represents a polytopic membrane protein composed of 11 transmembrane spanning domains. In parallel, a large aux1 allelic series containing null, partial-loss-of-function, and conditional mutations was characterized to identify the functionally important domains and amino acid residues within the AUX1 polypeptide. Whereas almost all partial-loss-of-function and null alleles cluster in the core permease region, the sole conditional allele aux1-7 modifies the function of the external C-terminal domain.




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