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Unfoldase-mediated protein translocation through an α-hemolysin nanopore
Open accessAbstract
Using nanopores to sequence biopolymers was proposed more than a decade ago. Recent advances in enzyme-based control of DNA translocation and in DNA nucleotide resolution using modified biological pores have satisfied two technical requirements of a functional nanopore DNA sequencing device. Nanopore sequencing of proteins was also envisioned. Although proteins have been shown to move through nanopores, a technique to unfold proteins for processive translocation has yet to be demonstrated. Here we describe controlled unfolding and translocation of proteins through the α-hemolysin (α-HL) pore using the AAA+ unfoldase ClpX. Sequence-dependent features of individual engineered proteins were detected during translocation. These results demonstrate that molecular motors can reproducibly drive proteins through a model nanopore—a feature required for protein sequence analysis using this single-molecule technology.
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Cited by
The Oxford Nanopore MinION: delivery of nanopore sequencing to the genomics community
Jain, M., Olsen, H. E., Paten, B., & Akeson, M. (2016) · Genome Biology · doi:10.1186/s13059-016-1103-0 · Cited by 1,588
Self-citationSingle-cell RNA-seq: advances and future challenges
Saliba, A.-E., Westermann, A. J., Gorski, S. A., & Vogel, J. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku555 · Cited by 847
“Briefly, in nanopore-based sequencing the identity and sequential order of nucleotides is determined as the nucleic acid molecule of interest is threaded through one of many tiny (nano)pores in a membrane (161–163 , 168).”
Nanopore-based technologies beyond DNA sequencing
Ying, Y.-L., Hu, Z.-L., Zhang, S., Qing, Y., Fragasso, A., Maglia, G., Meller, A., Bayley, H., Dekker, C., & Long, Y.-T. (2022) · Nature Nanotechnology · doi:10.1038/s41565-022-01193-2 · Cited by 538
Electrical recognition of the twenty proteinogenic amino acids using an aerolysin nanopore
Ouldali, H., Sarthak, K., Ensslen, T., Piguet, F., Manivet, P., Pelta, J., Behrends, J. C., Aksimentiev, A., & Oukhaled, A. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0345-2 · Cited by 474
Digitally encoded DNA nanostructures for multiplexed, single-molecule protein sensing with nanopores
Bell, N. A. W., & Keyser, U. F. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2016.50 · Cited by 345
Metadata
- Authors
- Nivala, J., Marks, D. B., & Akeson, M.
- Venue
- Nature Biotechnology
- Published
- 2013-02-03
- Volume
- 31
- Issue
- 3
- Pages
- 247-250
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W2085532083
- Cited by
- 361
- References
- 0
- FWCI
- 16.83
- Type
- journal article
- Language
- en
- Open access
- green
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