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J. Biol. Chem., Vol. 280, Issue 11, 9773-9779, March 18, 2005

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-Amylase Is Not Required for Breakdown of Transitory Starch in Arabidopsis Leaves^*

From the ^aInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan, China, ^dInstitute of Plant Sciences, University of Bern, Altenbergrain 21, CH-3013 Bern, Switzerland, ^fInstitute of Molecular Plant Sciences, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JH, United Kingdom, ^hDepartment of Metabolic Biology, John Innes Centre, Colney Lane, Norwich NR4 7UH, United Kingdom, and ^kDepartment of Botany, National Taiwan University, Taipei 106, Taiwan, China

The Arabidopsis thaliana genome encodes three -amylase-like proteins (AtAMY1, AtAMY2, and AtAMY3). Only AtAMY3 has a predicted N-terminal transit peptide for plastidial localization. AtAMY3 is an unusually large -amylase (93.5 kDa) with the C-terminal half showing similarity to other known -amylases. When expressed in Escherichia coli, both the whole AtAMY3 protein and the C-terminal half alone show -amylase activity. We show that AtAMY3 is localized in chloroplasts. The starch-excess mutant of Arabidopsis sex4, previously shown to have reduced plastidial -amylase activity, is deficient in AtAMY3 protein. Unexpectedly, T-DNA knock-out mutants of AtAMY3 have the same diurnal pattern of transitory starch metabolism as the wild type. These results show that AtAMY3 is not required for transitory starch breakdown and that the starch-excess phenotype of the sex4 mutant is not caused simply by deficiency of AtAMY3 protein. Knock-out mutants in the predicted non-plastidial -amylases AtAMY1 and AtAMY2 were also isolated, and these displayed normal starch breakdown in the dark as expected for extraplastidial amylases. Furthermore, all three AtAMY double knock-out mutant combinations and the triple knock-out degraded their leaf starch normally. We conclude that -amylase is not necessary for transitory starch breakdown in Arabidopsis leaves.

Received for publication, December 3, 2004 , and in revised form, January 6, 2005.

^* The John Innes Centre is supported by a competitive strategic grant from the Biotechnology and Biological Science Research Council. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^b Current address: Section of Plant Biology, 1231 Life Sciences Addition, University of California, Davis, CA 95616.

^c These authors contributed equally to this work.

^e Supported by the National Centre of Competence in Research-Plant Survival (National Science Foundation, Switzerland).

ⁱ Supported by a European Union Leonardo da Vinci award.

^j Supported by an award from the Science and Technology Agency of Japan. Current address: Rice Physiology Laboratory, Dept. of Rice Research, National Institute of Crop Science, Tsukuba, Ibaraki 305-8518, Japan.

^l Supported by Biotechnology and Biological Science Research Council of the United Kingdom Grants D11089, D11090, and D16789.

^m Supported by Grant NSC 88-2311-B-001-034 from the National Science Council, Taiwan, China, and Academia Sinica, Taipei, Taiwan.

^g To whom correspondence should be addressed: Institute of Molecular Plant Sciences, University of Edinburgh, Mayfield Rd., Edinburgh EH9 3JH, UK. Tel.: 44-131-650-5316; Fax: 44-131-650-5392; E-mail: daniel.fulton{at}ed.ac.uk.

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