First published online January 30, 2003; 10.1104/pp.016519
Plant Physiol, March 2003, Vol. 131, pp. 1178-1190
Analysis of the Plastidic phosphate translocator Gene
Family in Arabidopsis and Identification of New phosphate
translocator-Homologous Transporters, Classified by Their
Putative Substrate-Binding Site1
Silke
Knappe,
Ulf-Ingo
Flügge, and
Karsten
Fischer*
Botanisches Institut der Universität zu Köln, Lehrstuhl
II, Gyrhofstrasse 15, D-50931 Cologne, Germany
Analysis of the Arabidopsis genome revealed the complete set
of plastidic phosphate translocator (pPT)
genes. The Arabidopsis genome contains 16 pPT genes:
single copies of genes coding for the triose phosphate/phosphate
translocator and the xylulose phosphate/phosphate translocator, and two
genes coding for each the phosphoenolpyruvate/phosphate translocator and the glucose-6-phosphate/phosphate translocator. A
relatively high number of truncated
phosphoenolpyruvate/phosphate translocator genes (six)
and glucose-6-phosphate/phosphate translocator genes
(four) could be detected with almost conserved intron/exon structures
as compared with the functional genes. In addition, a variety of
PT-homologous (PTh) genes could be
identified in Arabidopsis and other organisms. They all belong to the
drug/metabolite transporter superfamily showing significant
similarities to nucleotide sugar transporters (NSTs). The pPT, PTh, and
NST proteins all possess six to eight transmembrane helices. According
to the analysis of conserved motifs in these proteins, the PTh proteins
can be divided into (a) the lysine (Lys)/arginine group comprising only non-plant proteins, (b) the Lys-valine/alanine/glycine group of Arabidopsis proteins, (c) the Lys/asparagine group of Arabidopsis proteins, and (d) the Lys/threonine group of plant and non-plant proteins. None of these proteins have been characterized so far. The
analysis of the putative substrate-binding sites of the pPT, PTh, and
NST proteins led to the suggestion that all these proteins share common
substrate-binding sites on either side of the membrane each of which
contain a conserved Lys residue.
1
This work was supported by the Deutsche Forschungsgemeinschaft.
*
Corresponding author; e-mail karsten.fischer{at}uni-koeln.de;
fax 49-221-470-5039.
© 2003 American Society of Plant Biologists
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