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Label-Free and Real-Time Detection of Protein Ubiquitination with a Biological Nanopore

Wloka, C., Van Meervelt, V., van Gelder, D., Danda, N., Jager, N., Williams, C. P. & Maglia, G., Apr-2017, In : Acs Nano. 11, 5, p. 4387-4394 8 p., acsnano.6b07760.

Research output: Contribution to journalArticleAcademicpeer-review

The covalent addition of ubiquitin to target proteins is a key post-translational modification that is linked to a myriad of biological processes. Here, we report a fast, single-molecule, and label-free method to probe the ubiquitination of proteins employing an engineered Cytolysin A (ClyA) nanopore. We show that ionic currents can be used to recognize mono- and polyubiquitinated forms of native proteins under physiological conditions. Using defined conjugates, we also show that isomeric monoubiquitinated proteins can be discriminated. The nanopore approach allows following the ubiquitination reaction in real time, which will accelerate the understanding of fundamental mechanisms linked to protein ubiquitination.

Original languageEnglish
Article numberacsnano.6b07760
Pages (from-to)4387-4394
Number of pages8
JournalAcs Nano
Volume11
Issue number5
Early online dateMar-2017
Publication statusPublished - Apr-2017

    Keywords

  • nanotechnology, nanopore, single-molecule kinetics, protein modifications, ubiquitin, MOLECULE COVALENT CHEMISTRY, PORE, TRANSLOCATION, REVEALS, DISEASE, DNA, DISCRIMINATION, IDENTIFICATION, MECHANISMS, VARIANTS

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