Ribosome-inactivating lectins of plants
Juri V. Kozlov, O. J. Sudarkina, A. G. Kurmanova
Abstract
Juri V. Kozlov, O. J. Sudarkina, A. G. Kurmanova
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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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.
Key concepts: Ribosome-inactivating protein, Ricin, Ribosome, Depurination, Biochemistry, Protein subunit, Trichosanthin, Protein biosynthesis