Proteins Membrane Binding and Pore Formation

  • Gregor Anderluh
  • Jeremy Lakey

Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 677)

Table of contents

  1. Front Matter
    Pages i-xix
  2. Susanne C. Feil, Galina Polekhina, Michael A. Gorman, Michael W. Parker
    Pages 1-13
  3. Gustavo Fuertes, Diana Giménez, Santi Esteban-Martín, Ana J. García-Sáez, Orlando Sánchez, Jesús Salgado
    Pages 31-55
  4. Robert J. C. Gilbert
    Pages 56-66
  5. José Miguel Mancheño, Hiroaki Tateno, Daniel Sher, Irwin J. Goldstein
    Pages 67-80
  6. Helen Ridleya, Christopher L. Johnson, Jeremy H. Lakey
    Pages 81-90
  7. Ana J. García-Sáez, Gustavo Fuertes, Jacob Suckale, Jesús Salgado
    Pages 91-105
  8. Stuart Hunt, Jeffrey Green, Peter J. Artymiuk
    Pages 116-126
  9. Mario Soberón, Liliana Pardo, Carlos Muñóz-Garay, Jorge Sánchez, Isabel Gómez, Helena Porta et al.
    Pages 127-142
  10. Wen-guey Wu, Siu-Cin Tjong, Po-long Wu, Je-hung Kuo, Karen Wu
    Pages 143-149
  11. Bruce L. Kagan, Jyothi Thundimadathil
    Pages 150-167
  12. Back Matter
    Pages 169-172

About this book

Introduction

Formation of transmembrane pores is a very effective way of killing cells. It is thus not surprising that many bacterial and eukaryotic toxic agents are pore-forming proteins. Pore formation in a target membrane is a complex process composed of several steps; proteins need to attach to the lipid membrane, possibly aggregate in the plane of the membrane and finally form a pore by inserting part of the polypeptide chain across the lipid bilayer. Structural information about toxins at each stage is indispensible for the biochemical and molecular biological studies that aim to - derstand how pores are formed at the molecular level. There are currently only two Staphylococcus aureus and hemolysin E from Escherichia coli. Therefore, what we know about these proteins was obtained over many years of intense experimentation. We have nevertheless, in the last couple of years, witnessed a significant rise in structural information on the soluble forms of pore-forming proteins. Surprisingly, many unexpected similarities with other proteins were noted, despite extremely low or insignificant sequence similarity. It appears that lipid membrane binding and formation of transmembrane channels is achieved in many cases by a limited repertoire of structures. This book describes how several of the important pore forming toxin families achieve membrane bi- ing and which structural elements are used for formation of transmembrane pores. Our contributors have thus provided the means for a comparative analysis of several unrelated families.

Keywords

Anderluh Lakey Pore membrane peptides protein proteins

Editors and affiliations

  • Gregor Anderluh
    • 1
  • Jeremy Lakey
    • 2
  1. 1.Department of BiologyUniversity of LjubljanaLjubljanaSlovenia
  2. 2.Institute for Cell and Molecular Biosciences, The Medical SchoolUniversity of Newcastle upon TyneNewcastle upon TyneUK

Bibliographic information

  • DOI https://doi.org/10.1007/978-1-4419-6327-7
  • Copyright Information Landes Bioscience and Springer Science+Business Media, LLC 2010
  • Publisher Name Springer, New York, NY
  • eBook Packages Biomedical and Life Sciences
  • Print ISBN 978-1-4419-6326-0
  • Online ISBN 978-1-4419-6327-7
  • Series Print ISSN 0065-2598
  • About this book