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TitleA dual-constriction biological nanopore resolves homonucleotide sequences with high fidelity.
Journal, issue, pagesNat Biotechnol, Vol. 38, Issue 12, Page 1415-1420, Year 2020
Publish dateJul 6, 2020
AuthorsSander E Van der Verren / Nani Van Gerven / Wim Jonckheere / Richard Hambley / Pratik Singh / John Kilgour / Michael Jordan / E Jayne Wallace / Lakmal Jayasinghe / Han Remaut /
PubMed AbstractSingle-molecule long-read DNA sequencing with biological nanopores is fast and high-throughput but suffers reduced accuracy in homonucleotide stretches. We now combine the CsgG nanopore with the 35- ...Single-molecule long-read DNA sequencing with biological nanopores is fast and high-throughput but suffers reduced accuracy in homonucleotide stretches. We now combine the CsgG nanopore with the 35-residue N-terminal region of its extracellular interaction partner CsgF to produce a dual-constriction pore with improved signal and base-calling accuracy for homopolymer regions. The electron cryo-microscopy structure of CsgG in complex with full-length CsgF shows that the 33 N-terminal residues of CsgF bind inside the β-barrel of the pore, forming a defined second constriction. In complexes of CsgG bound to a 35-residue CsgF constriction peptide, the second constriction is separated from the primary constriction by ~25 Å. We find that both constrictions contribute to electrical signal modulation during single-stranded DNA translocation. DNA sequencing using a prototype CsgG-CsgF protein pore with two constrictions improved single-read accuracy by 25 to 70% in homopolymers up to 9 nucleotides long.
External linksNat Biotechnol / PubMed:32632300 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

10206

6si7

EMDB-10206, PDB-6si7:
Structure of the curli secretion-assembly complex CsgG:CsgF
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • escherichia coli (E. coli)
KeywordsPROTEIN TRANSPORT / Secretion Channel / Curli / Outer Membrane Protein / Nanopore Sensing / Bacterial amyloid

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