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Protein translocation through an a-hemolysin-caseinolytic peptidase X homolog (ClpX) nanopore system

A method to translocate proteins through a-hemolysin nanopores could eventually enable nanopore-based protein sequencing. There are nanopore-based DNA sequencing methods in commercial development that detect and identify DNA by measuring voltage changes as individual base pairs pass through a membrane-embedded nanopore, but these methods cannot identify peptides. To enable protein translocation through a membrane-embedded nanopore, the AAA+ unfoldase ClpX was added in solution to one side of the membrane, allowing detection of structure-dependent voltage changes as a protein substrate of about 100 amino acids and carrying a ClpX binding tag passed through the pore. Next steps could include determining the relationship between voltage change and amino acid identity.
At least five companies are developing nanopore-based DNA sequencing systems.

SciBX 6(6); doi:10.1038/scibx.2013.147
Published online Feb. 14, 2013

Patent and licensing status undisclosed

Nivala, J. et al. Nat. Biotechnol.; published online Feb. 3, 2013;
doi:10.1038/nbt.2503
Contact: Mark Akeson, University of California, Santa Cruz, Calif.
e-mail:

makeson@soe.ucsc.edu