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First published online July 2, 2004; 10.1104/pp.104.042184

Plant Physiology 135:1367-1377 (2004)
© 2004 American Society of Plant Biologists

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CELL BIOLOGY AND SIGNAL TRANSDUCTION

Signal Peptide-Dependent Targeting of a Rice {alpha}-Amylase and Cargo Proteins to Plastids and Extracellular Compartments of Plant Cells1

Min-Huei Chen2,3, Li-Fen Huang2,4, Hsou-min Li, Yung-Reui Chen and Su-May Yu*

Institute of Molecular Biology, Academia Sinica, Nankang, Taipei, 11529 Taiwan, Republic of China (M.-H.C., L.-F.H., H.-m.L., S.-M.Y.); and Department of Botany, National Taiwan University, Taipei, 10764 Taiwan, Republic of China (M.-H.C., Y.-R.C.)

{alpha}-Amylases are important enzymes for starch degradation in plants. However, it has been a long-running debate as to whether {alpha}-amylases are localized in plastids where starch is stored. To study the subcellular localization of {alpha}-amylases in plant cells, a rice (Oryza sativa) {alpha}-amylase, {alpha}Amy3, with or without its own signal peptide (SP) was expressed in transgenic tobacco (Nicotiana tabacum) and analyzed. Loss-of-function analyses revealed that SP was required for targeting of {alpha}Amy3 to chloroplasts and/or amyloplasts and cell walls and/or extracellular compartments of leaves and suspension cells. SP was also required for in vitro transcribed and/or translated {alpha}Amy3 to be cotranslationally imported and processed in canine microsomes. {alpha}Amy3, present in chloroplasts of transgenic tobacco leaves, was processed to a product with Mr similar to {alpha}Amy3 minus its SP. Amino acid sequence analysis revealed that the SP of chloroplast localized {alpha}Amy3 was cleaved at a site only one amino acid preceding the predicted cleavage site. Function of the {alpha}Amy3 SP was further studied by gain-of-function analyses. {beta}-Glucuronidase (GUS) and green fluorescence protein fused with or without the {alpha}Amy3 SP was expressed in transgenic tobacco or rice. The {alpha}Amy3 SP directed translocation of GUS and green fluorescence protein to chloroplasts and/or amyloplasts and cell walls in tobacco leaves and rice suspension cells. The SP of another rice {alpha}-amylase, {alpha}Amy8, similarly directed the dual localizations of GUS in transgenic tobacco leaves. This study is the first evidence of SP-dependent dual translocations of proteins to plastids and extracellular compartments, which provides new insights into the role of SP in protein targeting and the pathways of SP-dependent protein translocation in plants.

1 This work was supported by Academia Sinica of the Republic of China.

2 These authors contributed equally to the paper.

3 Present address: Department of Biochemistry, Life Science Building, SUNY at Stony Brook, Life Science Building, Stony Brook, NY 11794.

4 Present address: Program in Plant Molecular and Cellular Biology, Department of Horticultural Sciences, University of Florida, Gainesville, FL 32611.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.042184.

* Corresponding author; e-mail sumay{at}imb.sinica.edu.tw; fax 886–2–2788–2695 or 886–2–2782–6085.

Received March 6, 2004; returned for revision April 5, 2004; accepted April 6, 2004.




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