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J. Biol. Chem., Vol. 283, Issue 48, 33276-33286, November 28, 2008

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Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism^*

Kerry L. Chamberlain¹², Richard S. Marshall¹³, Nicholas A. Jolliffe, Lorenzo Frigerio, Aldo Ceriotti, J. Michael Lord, and Lynne M. Roberts⁴

From the Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, United Kingdom and the Istituto di Biologia e Biotecnologia Agraria, Consiglio Nazionale delle Ricerche, via Bassini 15, 20133 Milano, Italy

The B chain of ricin was expressed and delivered to the endoplasmic reticulum of tobacco protoplasts where it disappeared with time in a manner consistent with degradation. This turnover did not occur in the vacuoles or upon secretion. Indeed, several lines of evidence indicate that, in contrast to the turnover of endoplasmic reticulum-targeted ricin A chain in the cytosol, the bulk of expressed ricin B chain was degraded in the secretory pathway.

Received for publication, July 9, 2008 , and in revised form, September 19, 2008.

^* This work was supported in part by Wellcome Trust Programme Grant 080566/Z/06/Z (to L. M. R. and J. M. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

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¹ Both authors contributed equally to this work.

² Supported by a Wellcome Trust Prize Studentship.

³ Supported by a studentship from the UK Biotechnology and Biological Sciences Research Council.

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⁴ To whom correspondence should be addressed. Fax: 44-2476-523701; E-mail: lynne.roberts{at}warwick.ac.uk.

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