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Plant Cell Advance Online Publication
Published on October 13, 2006; 10.1105/tpc.106.042226

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Received March 2, 2006
Returned for revision July 21, 2006
Accepted September 19, 2006

Retention of a Bean Phaseolin/Maize {gamma}-Zein Fusion in the Endoplasmic Reticulum Depends on Disulfide Bond Formation

Andrea Pompa 1 and Alessandro Vitale 1*

1 Istituto di Biologia e Biotecnologia Agraria, Consiglio Nazionale delle Ricerche, 20133 Milano, Italy

* To whom correspondence should be addressed. E-mail: vitale{at}ibba.cnr.it.

Most seed storage proteins of the prolamin class accumulate in the endoplasmic reticulum (ER) as large insoluble polymers termed protein bodies (PBs), through mechanisms that are still poorly understood. We previously showed that a fusion between the Phaseolus vulgaris vacuolar storage protein phaseolin and the N-terminal half of the Zea mays prolamin {gamma}-zein forms ER-located PBs. Zeolin has 6 Cys residues and, like {gamma}-zein with 15 residues, is insoluble unless reduced. The contribution of disulfide bonds to zeolin destiny was determined by studying in vivo the effects of 2-mercaptoethanol (2-ME) and by zeolin mutagenesis. We show that in tobacco (Nicotiana tabacum) protoplasts, 2-ME enhances interactions of newly synthesized proteins with the ER chaperone BiP and inhibits the secretory traffic of soluble proteins with or without disulfide bonds. In spite of this general inhibition, 2-ME enhances the solubility of zeolin and relieves its retention in the ER, resulting in increased zeolin traffic. Consistently, mutated zeolin unable to form disulfide bonds is soluble and efficiently enters the secretory traffic without 2-ME treatment. We conclude that disulfide bonds that lead to insolubilization are a determinant for PB-mediated protein accumulation in the ER.




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The human immunodeficiency virus antigen Nef forms protein bodies in leaves of transgenic tobacco when fused to zeolin
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