Research Highlight
Published: 14 October 2024
Sequencing
Iris Marchal 1
Nature Biotechnology
volume 42, page 1499 (2024)Cite this article
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Understanding proteomic diversity at the molecular level is essential for advances in biology and medicine, but sequencing proteins in their full, native form remains challenging. A study in Nature by Motone et al. introduces a nanopore sequencing method that can read single, full-length protein molecules, enabling the detection of single amino acid substitutions and post-translational modifications (PTMs).
The method involves a two-step process. First, a protein is loaded into a nanopore formed by the bacterial lipoprotein CsgC by electrophoretic force, facilitated by a negatively charged tail domain and the addition of a ‘stopper’ sequence. Then, ClpX unfoldase steadily pulls it back through in a trans-to-cis direction. Using synthetic proteins, the authors show their method can detect single amino acid substitutions and can map the activity of kinases, identifying site-specific PTMs such as phosphorylation.
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Nature Biotechnology https://www.nature.com/nbt/
Iris Marchal
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Cite this article
Marchal, I. A strategy to load, rethread and read protein sequences through a nanopore.
Nat Biotechnol 42, 1499 (2024). https://doi.org/10.1038/s41587-024-02443-5
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Published: 14 October 2024
Issue Date: October 2024
DOI : https://doi.org/10.1038/s41587-024-02443-5
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