J. Michael Lord

Martin R. Hartley

Many plants produce enzymes collectively known as ribosome-inactivating proteins (RIPs). RIPs catalyze the removal of an adenine residue from a conserved loop in the large ribosomal RNA. The adenine residue removed by this depurination is crucial for the binding of elongation factors. Ribosomes modified in this way are no longer able to carry out protein synthesis. Most RIPs exist as single polypeptides (Type 1 RIPs) which are largely non-toxic to mammalian cells because they are unable to enter them and thus cannot reach their ribosomal substrate. In some instances, however, the RIP forms part of a heterodimer where its partner polypeptide is a lectin (Type 2 RIPs). These heterodimeric RIPs are able to bind to and enter mammalian cells. Their ability to reach and modify ribosomes in target cells means these proteins are some of the most potently cytotoxic poisons found in nature, and are widely assumed to play a protective role as part of the host plant’s defenses. RIPs are able to further damage target cells by inducing apoptosis. In addition, certain plants produce lectins lacking an RIP component but which are also cytotoxic. This book focuses on the structure/function and some potential applications of these toxic plant proteins.

Toxic Plant Proteins

John Davey

Mike Lord

Volume 1 of this two volume set focuses on techniques for studying cell structure. It describes light and electron microscopy, subcellular fractionation, protein purification and analysis, nucleic acid analysis, lipid analysis, and investigations of the cytoskeleton. Volume 2 concentrates on understanding how cells function. It describes a range of key investigations of cell function including analyses of gene expression, the cell cycle, cellular bioenergetics, transport across the nuclear membrane and the ER membrane, endosome transport, receptors, and signal transduction.

J. Michael Lord

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