Format

Send to

Choose Destination
Biophys J. 2011 Dec 7;101(11):2679-83. doi: 10.1016/j.bpj.2011.09.054.

Rapid assembly of a multimeric membrane protein pore.

Author information

1
Department of Chemistry, University of Oxford, Oxford, United Kingdom.

Abstract

We have observed the assembly of the staphylococcal pore-forming toxin α-hemolysin using single-molecule fluorescence imaging. Surprisingly, assembly from the monomer to the complete heptamer is extremely rapid, occurring in <5 ms. No lower order oligomeric intermediates are detected. Monte Carlo simulation of our experiment shows that assembly is diffusion limited, and pore formation is dependent on the stability of intermediate species. There are close similarities between bacterial pore-forming toxins, such as staphylococcal α-hemolysin, the anthrax protective antigen, and the cholesterol-dependent cytolysins, and their eukaryotic analogs, such as the complement pore membrane attack complex and perforin domain. The assembly mechanism we have observed for α-hemolysin provides a simple model that aids our understanding of these important pore formers.

PMID:
22261056
PMCID:
PMC3297801
DOI:
10.1016/j.bpj.2011.09.054
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center