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Ribosome-inactivating lectins of plants

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Abstract

A heterogeneous group of plant proteins are capable of enzymatically inactivating ribosomes by depurination of the invariant adenine in the 28S rRNA. Some of these proteins are heterodimers, containing a lectin subunit joined to an enzymatic subunit via a disulfide bond. Ricin and abrin, which are among the most toxic substances known, belong to this class of heterodimeric proteins. The review focuses on the structure of plant heterodimeric ribosome-inactivating proteins, the way of their action on the ribosome, biosynthesis, intracellular trafficking, and potential applications in medicine.

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Authors and Affiliations

  1. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991, Russia

    J. V. Kozlov, O. J. Sudarkina & A. G. Kurmanova

  2. Center of Medical Research, University of Oslo, Moscow, 119334, Russia

    J. V. Kozlov, O. J. Sudarkina & A. G. Kurmanova

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  1. J. V. Kozlov
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  2. O. J. Sudarkina
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  3. A. G. Kurmanova
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Original Russian Text © J.V. Kozlov, O.J. Sudarkina, A.G. Kurmanova, 2006, published in Molekulyarnaya Biologiya, 2006, Vol. 40, No. 4, pp. 711–723.

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Kozlov, J.V., Sudarkina, O.J. & Kurmanova, A.G. Ribosome-inactivating lectins of plants. Mol Biol 40, 635–646 (2006). https://doi.org/10.1134/S0026893306040169

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