Sub-angstrom single-molecule measurements of motor proteins using a nanopore

Present techniques for measuring the motion of single motor proteins, such as FRET and optical tweezers, are limited to a resolution of ~300 pm. We use ion current modulation through the protein nanopore MspA to observe translocation of helicase Hel308 on DNA with up to ~40 picometer sensitivity. Th...

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Detalles Bibliográficos
Autores principales: Derrington, Ian M, Craig, Jonathan M, Stava, Eric, Laszlo, Andrew H, Ross, Brian C, Brinkerhoff, Henry, Nova, Ian C, Doering, Kenji, Tickman, Benjamin I, Ronaghi, Mostafa, Mandell, Jeffrey G, Gunderson, Kevin L, Gundlach, Jens H
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4915380/
https://www.ncbi.nlm.nih.gov/pubmed/26414351
http://dx.doi.org/10.1038/nbt.3357
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author Derrington, Ian M
Craig, Jonathan M
Stava, Eric
Laszlo, Andrew H
Ross, Brian C
Brinkerhoff, Henry
Nova, Ian C
Doering, Kenji
Tickman, Benjamin I
Ronaghi, Mostafa
Mandell, Jeffrey G
Gunderson, Kevin L
Gundlach, Jens H
author_facet Derrington, Ian M
Craig, Jonathan M
Stava, Eric
Laszlo, Andrew H
Ross, Brian C
Brinkerhoff, Henry
Nova, Ian C
Doering, Kenji
Tickman, Benjamin I
Ronaghi, Mostafa
Mandell, Jeffrey G
Gunderson, Kevin L
Gundlach, Jens H
author_sort Derrington, Ian M
collection PubMed
description Present techniques for measuring the motion of single motor proteins, such as FRET and optical tweezers, are limited to a resolution of ~300 pm. We use ion current modulation through the protein nanopore MspA to observe translocation of helicase Hel308 on DNA with up to ~40 picometer sensitivity. This approach should be applicable to any protein that translocates on DNA or RNA, including helicases, polymerases, recombinases and DNA repair enzymes.
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spelling pubmed-49153802016-06-21 Sub-angstrom single-molecule measurements of motor proteins using a nanopore Derrington, Ian M Craig, Jonathan M Stava, Eric Laszlo, Andrew H Ross, Brian C Brinkerhoff, Henry Nova, Ian C Doering, Kenji Tickman, Benjamin I Ronaghi, Mostafa Mandell, Jeffrey G Gunderson, Kevin L Gundlach, Jens H Nat Biotechnol Article Present techniques for measuring the motion of single motor proteins, such as FRET and optical tweezers, are limited to a resolution of ~300 pm. We use ion current modulation through the protein nanopore MspA to observe translocation of helicase Hel308 on DNA with up to ~40 picometer sensitivity. This approach should be applicable to any protein that translocates on DNA or RNA, including helicases, polymerases, recombinases and DNA repair enzymes. 2015-09-28 2015-10 /pmc/articles/PMC4915380/ /pubmed/26414351 http://dx.doi.org/10.1038/nbt.3357 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Derrington, Ian M
Craig, Jonathan M
Stava, Eric
Laszlo, Andrew H
Ross, Brian C
Brinkerhoff, Henry
Nova, Ian C
Doering, Kenji
Tickman, Benjamin I
Ronaghi, Mostafa
Mandell, Jeffrey G
Gunderson, Kevin L
Gundlach, Jens H
Sub-angstrom single-molecule measurements of motor proteins using a nanopore
title Sub-angstrom single-molecule measurements of motor proteins using a nanopore
title_full Sub-angstrom single-molecule measurements of motor proteins using a nanopore
title_fullStr Sub-angstrom single-molecule measurements of motor proteins using a nanopore
title_full_unstemmed Sub-angstrom single-molecule measurements of motor proteins using a nanopore
title_short Sub-angstrom single-molecule measurements of motor proteins using a nanopore
title_sort sub-angstrom single-molecule measurements of motor proteins using a nanopore
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4915380/
https://www.ncbi.nlm.nih.gov/pubmed/26414351
http://dx.doi.org/10.1038/nbt.3357
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