Toxic Plant Proteins

  • J. Michael Lord
  • Martin R. Hartley

Part of the Plant Cell Monographs book series (CELLMONO, volume 18)

Table of contents

  1. Front Matter
    Pages i-x
  2. Willy J. Peumans, Els J. M. Van Damme
    Pages 1-26
  3. Kazuyuki Takai, Tatsuya Sawasaki, Yaeta Endo
    Pages 27-39
  4. Alessio Lombardi, Richard S. Marshall, Carmelinda Savino, Maria Serena Fabbrini, Aldo Ceriotti
    Pages 55-78
  5. Augusto Parente, Rita Berisio, Angela Chambery, Antimo Di Maro
    Pages 79-106
  6. José Miguel Ferreras, Lucía Citores, Rosario Iglesias, Pilar Jiménez, Tomás Girbés
    Pages 107-131
  7. Ana Paula Ulian Araújo, Priscila Vasques Castilho, Leandro Seiji Goto
    Pages 133-147
  8. Carlotta Balconi, Chiara Lanzanova, Mario Motto
    Pages 149-166
  9. Deepa Sikriwal, Janendra K. Batra
    Pages 167-189
  10. Lorenzo Frigerio, Lynne M. Roberts
    Pages 191-205
  11. Robert A. Spooner, Jonathan P. Cook, Shuyu Li, Paula Pietroni, J. Michael Lord
    Pages 207-224
  12. Giulio Fracasso, Fiorenzo Stirpe, Marco Colombatti
    Pages 225-263
  13. Back Matter
    Pages 265-270

About this book

Introduction

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.

Keywords

Cytosol Polypeptide Protein RNA Ribosome-inactivating proteins Tree enzymes plant lectins proteins ricinus communis

Editors and affiliations

  • J. Michael Lord
    • 1
  • Martin R. Hartley
    • 2
  1. 1.Dept. Biological SciencesUniversity of WarwickCoventryUnited Kingdom
  2. 2.Dept. Biological SciencesUniversity of WarwickCoventryUnited Kingdom

Bibliographic information

  • DOI https://doi.org/10.1007/978-3-642-12176-0
  • Copyright Information Springer-Verlag Berlin Heidelberg 2010
  • Publisher Name Springer, Berlin, Heidelberg
  • eBook Packages Biomedical and Life Sciences
  • Print ISBN 978-3-642-12175-3
  • Online ISBN 978-3-642-12176-0
  • Series Print ISSN 1861-1370
  • Series Online ISSN 1861-1362
  • About this book