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Plant Physiol, November 2001, Vol. 127, pp. 1212-1223

Native and Artificial Reticuloplasmins Co-Accumulate in Distinct Domains of the Endoplasmic Reticulum and in Post-Endoplasmic Reticulum Compartments1

Esperanza Torres, Pablo Gonzalez-Melendi, Eva Stöger, Peter Shaw, Richard M. Twyman, Liz Nicholson, Carmen Vaquero, Rainer Fischer, Paul Christou, and Yolande Perrin2*

Molecular Biotechnology Unit (E.T., P.G.-M., E.S., R.M.T., L.N., P.C., Y.P.) and Cell Biology Department (P.G.-M., P.S.), John Innes Centre, Colney Lane, Norwich NR4 7UH, United Kingdom; Institut für Biologie I (Botanic/Molekulargenetik), RWTH Aachen, Worringerweg 1, D-52074 Aachen, Germany (C.V., R.F.); and Fraunhofer Abteilung für Molekulare Biotechnologie, IUTC, Grafschaft, Auf dem Aberg 1, D-57392 Schmallenberg, Germany (R.F.)

We compared the subcellular distribution of native and artificial reticuloplasmins in endosperm, callus, and leaf tissues of transgenic rice (Oryza sativa) to determine the distribution of these proteins among endoplasmic reticulum (ER) and post-ER compartments. The native reticuloplasmin was calreticulin. The artificial reticuloplasmin was a recombinant single-chain antibody (scFv), expressed with an N-terminal signal peptide and the C-terminal KDEL sequence for retrieval to the ER (scFvT84.66-KDEL). We found that both molecules were distributed in the same manner. In endosperm, each accumulated in ER-derived prolamine protein bodies, but also in glutelin protein storage vacuoles, even though glutelins are known to pass through the Golgi apparatus en route to these organelles. This finding may suggest that similar mechanisms are involved in the sorting of reticuloplasmins and rice seed storage proteins. However, the presence of reticuloplasmins in protein storage vacuoles could also be due to simple dispersal into these compartments during protein storage vacuole biogenesis, before glutelin deposition. In callus and leaf mesophyll cells, both reticuloplasmins accumulated in ribosome-coated vesicles probably derived directly from the rough ER.

1 This work was supported in part by the Instituto Colombiano para el Desarrollo de la Ciencia y la Technología "Francisco José de Caldas" (COLENCIAS; PhD fellowship to E.T.).

2 Present address: Université de Technologie de Compiègne, Unité Mixte de Recherche 6022 Centre National de la Recherche Scientifique, BP 20529-60205 Compiègne cedex, France.

* Corresponding author; e-mail yolande.perrin{at}utc.fr; fax 33-0-344-234300.

© 2001 American Society of Plant Physiologists


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