ricin/nicotiana

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Induction of Male Sterility in Tobacco by Anther-Specific Expression of the Gene for Ricin Enzymatic Subunit A Chain RTA.

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Targeted gene expression in plants allows us to further study biological traits of interest, such as reproductive and developmental processes. Here, the tobacco TA29 anther-specific promoter was used to direct the expression of the ricin enzymatic subunit A (RTA) in transgenic tobacco plants,

Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features.

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Proteins that fail to fold in the endoplasmic reticulum (ER) or cannot find a pattern for assembly are often disposed of by a process named ER-associated degradation (ERAD), which involves transport of the substrate protein across the ER membrane (dislocation) followed by rapid proteasome-mediated

The internal propeptide of the ricin precursor carries a sequence-specific determinant for vacuolar sorting.

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Ricin is a heterodimeric toxin that accumulates in the storage vacuoles of castor bean (Ricinus communis) endosperm. Proricin is synthesized as a single polypeptide precursor comprising the catalytic A chain and the Gal-binding B chain joined by a 12-amino acid linker propeptide. Upon arrival in the

Expression of functional hexahistidine-tagged ricin B in tobacco.

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Ricin B (RTB), the lectin subunit of ricin, shows promise as an effective mucosal adjuvant and carrier for use in humans. In order to obtain a recombinant plant source of RTB that is devoid of the toxic ricin A subunit, we expressed RTB in Nicotiana tabacum. RTB was engineered with an N-terminal

Identification of a glycosylphosphatidylinositol-anchored plasma membrane protein interacting with the C-terminus of auxin-binding protein 1: a photoaffinity crosslinking study.

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Synthetic peptides corresponding to the C-terminus of auxin-binding protein 1 (ABP1) have been shown to function as auxin agonists. To define a C-terminal receptor, photoaffinity crosslinking experiments were performed using an azido derivative of a C-terminal peptide and plasma membranes from maize

Preproricin expressed in Nicotiana tabacum cells in vitro is fully processed and biologically active.

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Ricin, the highly toxic glycoprotein expressed in the endosperm of castor seeds, is composed of a galactose-binding lectin B chain (RTB) disulfide linked to a RNA N-glycosidase A chain (RTA). Chemically modified ricin has been conjugated to monoclonal antibodies and used for targeted therapy of

Isolation and characterization of an RIP (ribosome-inactivating protein)-like protein from tobacco with dual enzymatic activity.

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Ribosome-inactivating proteins (RIPs) are N-glycosidases that remove a specific adenine from the sarcin/ricin loop of the large rRNA, thus arresting protein synthesis at the translocation step. In the present study, a protein termed tobacco RIP (TRIP) was isolated from tobacco (Nicotiana tabacum)

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