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Zeolin. A New Recombinant Storage Protein Constructed Using Maize -Zein and Bean Phaseolin¹

Istituto di Biologia e Biotecnologia Agraria, Consiglio Nazionale delle Ricerche, 20133 Milano, Italy (D.M, M.R., M.A., S.V., A.P., A.V.); and Istituto di Genetica Vegetale, Consiglio Nazionale delle Ricerche, 06128 Perugia, Italy (M.B., F.D.M., S.A.)

The major seed storage proteins of maize (Zea mays) and bean (Phaseolus vulgaris), zein and phaseolin, accumulate in the endoplasmic reticulum (ER) and in storage vacuoles, respectively. We show here that a chimeric protein composed of phaseolin and 89 amino acids of -zein, including the repeated and the Pro-rich domains, maintains the main characteristics of wild-type -zein: It is insoluble unless its disulfide bonds are reduced and forms ER-located protein bodies. Unlike wild-type phaseolin, the protein, which we called zeolin, accumulates to very high amounts in leaves of transgenic tobacco (Nicotiana tabacum). A relevant proportion of the ER chaperone BiP is associated with zeolin protein bodies in an ATP-sensitive fashion. Pulse-chase labeling confirms the high affinity of BiP to insoluble zeolin but indicates that, unlike structurally defective proteins that also extensively interact with BiP, zeolin is highly stable. We conclude that the -zein portion is sufficient to induce the formation of protein bodies also when fused to another protein. Because the storage proteins of cereals and legumes nutritionally complement each other, zeolin can be used as a starting point to produce nutritionally balanced and highly stable chimeric storage proteins.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.046409.

^* Corresponding author; e-mail vitale{at}ibba.cnr.it; fax 39–0223699–411.

Received May 13, 2004; returned for revision June 29, 2004; accepted July 1, 2004.

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