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JXB Advance Access published online on February 14, 2005
Journal of Experimental Botany, doi:10.1093/jxb/eri114
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Journal of Experimental Botany © Society for Experimental Biology 2005; all rights reserved
Received July 15, 2004
Accepted December 25, 2004

RESEARCH PAPER

Cytoplasm and chloroplasts are not suitable subcellular locations for {beta}-zein accumulation in transgenic plants

Michele Bellucci 1 *, Francesca De Marchis 1 *, Roberta Mannucci 2, Ralph Bock 3, and Sergio Arcioni 1*

1 Institute of Plant Genetics, Research Division of Perugia, CNR, via della Madonna Alta, 130, 06128 Perugia, Italy
2 Department of Clinical and Experimental Medicine, Section of Internal Medicine and Oncology, Perugia University Medical School, Policlinico Monteluce, 06122 Perugia, Italy
3 Universitaet Münster, Institut für Biochemie und Biotechnologie der Pflanzen, Hindenburgplatz 55, D-48143 Münster, Germany; Max-Planck-Institut für Molekulare Pflanzenphysiologie, Am Muehlenberg 1, D-14476 Potsdam-Golm, Germany

* To whom correspondence should be addressed.
Sergio Arcioni, E-mail: sergio.arcioni{at}igv.cnr.it


  Abstract

Zeins, the main storage proteins of maize that accumulate in the endoplasmic reticulum of the endosperm cells, are particularly interesting because they are rich in the essential sulphur amino acids. Overexpression of certain zein genes in plants such as alfalfa would be expected to improve the nutritional characteristics of this crop. Recently, significant accumulation values have been reached, but still far from those considered useful for nutritional purposes. This study investigates whether targeting to compartments other than the endoplasmic reticulum (cytosol and chloroplasts) could result in increasing {beta}-zein accumulation in transgenic plants. To address {beta}-zein to the cytosol, the fragment which codes for the signal peptide has been removed. {beta}-zein has also been targeted to alfalfa and tobacco chloroplasts by a transit peptide signal. Both tobacco, as a model plant species, and alfalfa have been transformed with the assembled constructs. An alternative route to accumulate {beta}-zein in the chloroplasts is to synthesize {beta}-zein directly in the plastid lumen. Thus, the {beta}-zein gene has also been inserted into tobacco plastid DNA. The {beta}-zein gene in each different type of transformed plant was properly transcribed, as determined by northern blot analysis, but no accumulation of {beta}-zein was detected, either in the cytoplasm or in the chloroplasts of alfalfa and tobacco transformed plants. Therefore, it is concluded that chloroplasts and the cytosol are not favourable subcellular locations for zein protein accumulation.

Keywords: {beta}-zein; chloroplast; cytoplasm; green fluorescent protein; improved nutritional quality; plastome transformation; transgenic alfalfa.

*These authors contributed equally to this work.


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