Journal
JOURNAL OF BIOCHEMISTRY
Volume 136, Issue 5, Pages 563-567Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvh160
Keywords
cooperative assembly; membrane binding; oligomerization; pore-forming toxins; single-molecule imaging
Categories
Ask authors/readers for more resources
Bacterial beta-barrel pore-forming toxins are secreted as water-soluble monomeric proteins and assemble into beta-barrel-shaped pores/channels through membranes of target cells, causing cell death and lysis. The pore assemblies that undergo various intermediate stages are symbolized by the association of multi-subunit structures in cells. Crystal structures of water-soluble monomers and membrane-embedded oligomeric pores, and recent studies involving biochemical detection and direct visualization of the sequential assembly of the toxin monomers have solved the mystery of how the pores are formed. Here, we review the mechanism of the cooperative assembly of several toxins of interest to explain the nature of the activities of the toxins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available