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First published online August 6, 2004; 10.1104/pp.104.045203

Plant Physiology 135:2088-2097 (2004)
© 2004 American Society of Plant Biologists

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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

The lys5 Mutations of Barley Reveal the Nature and Importance of Plastidial ADP-Glc Transporters for Starch Synthesis in Cereal Endosperm1

Nicola J. Patron2,3, Boris Greber2,4, Brendan F. Fahy, David A. Laurie, Mary L. Parker and Kay Denyer*

John Innes Centre, Colney, Norfolk NR4 7UH, United Kingdom (N.J.P., B.G., D.A.L., B.F.F., K.D.); and Institute of Food Research, Colney, Norfolk NR4 7UA, United Kingdom (M.L.P.)

Much of the ADP-Glc required for starch synthesis in the plastids of cereal endosperm is synthesized in the cytosol and transported across the plastid envelope. To provide information on the nature and role of the plastidial ADP-Glc transporter in barley (Hordeum vulgare), we screened a collection of low-starch mutants for lines with abnormally high levels of ADP-Glc in the developing endosperm. Three independent mutants were discovered, all of which carried mutations at the lys5 locus. Plastids isolated from the lys5 mutants were able to synthesize starch at normal rates from Glc-1-P but not from ADP-Glc, suggesting a specific lesion in the transport of ADP-Glc across the plastid envelope. The major plastidial envelope protein was purified, and its sequence showed it to be homologous to the maize (Zea mays) ADP-Glc transporter BRITTLE1. The gene encoding this protein in barley, Hv.Nst1, was cloned, sequenced, and mapped. Like lys5, Hv.Nst1 lies on chromosome 6(6H), and all three of the lys5 alleles that were examined were shown to carry lesions in Hv.Nst1. Two of the identified mutations in Hv.Nst1 lead to amino acid substitutions in a domain that is conserved in all members of the family of carrier proteins to which Hv.NST1 belongs. This strongly suggests that Hv.Nst1 lies at the Lys5 locus and encodes a plastidial ADP-Glc transporter. The low-starch phenotype of the lys5 mutants shows that the ADP-Glc transporter is required for normal rates of starch synthesis. This work on Hv.NST1, together with the earlier work on BRITTLE1, suggests that homologous transporters are probably present in the endosperm of all cereals.

1 This work was supported by the Biotechnology and Biological Sciences Research Council (BBSRC), UK (competitive strategic grant to the John Innes Centre and IFR), and by the Leonardo da Vinci Placement Programme of the European Union.

2 These authors contributed equally to the paper.

3 Present address: Department of Botany, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.

4 Present address: Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.045203.

* Corresponding author; e-mail kay.denyer{at}bbsrc.ac.uk; fax 44–1603–450045.

Received April 26, 2004; returned for revision May 17, 2004; accepted June 11, 2004.




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