A streptavidin variant with slower biotin dissociation and increased mechanostability

Streptavidin binds biotin-conjugates with exceptional stability, but dissociation does occur and can be limiting in imaging, DNA amplification, and nanotechnology. We identified a mutant streptavidin, which we call traptavidin, showing ~10-fold slower biotin off-rate, increased mechanical strength,...

Descripción completa

Detalles Bibliográficos
Autores principales: Chivers, Claire E., Crozat, Estelle, Chu, Calvin, Moy, Vincent T., Sherratt, David J., Howarth, Mark
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2862113/
https://www.ncbi.nlm.nih.gov/pubmed/20383133
http://dx.doi.org/10.1038/nmeth.1450
_version_ 1782180694888284160
author Chivers, Claire E.
Crozat, Estelle
Chu, Calvin
Moy, Vincent T.
Sherratt, David J.
Howarth, Mark
author_facet Chivers, Claire E.
Crozat, Estelle
Chu, Calvin
Moy, Vincent T.
Sherratt, David J.
Howarth, Mark
author_sort Chivers, Claire E.
collection PubMed
description Streptavidin binds biotin-conjugates with exceptional stability, but dissociation does occur and can be limiting in imaging, DNA amplification, and nanotechnology. We identified a mutant streptavidin, which we call traptavidin, showing ~10-fold slower biotin off-rate, increased mechanical strength, and improved thermostability; this resilience should find diverse applications. We show that the motor protein FtsK could strip proteins from DNA, rapidly displacing streptavidin from biotinylated DNA; traptavidin resisted displacement and thus indicated the force generated by FtsK translocation.
format Text
id pubmed-2862113
institution National Center for Biotechnology Information
language English
publishDate 2010
record_format MEDLINE/PubMed
spelling pubmed-28621132010-11-01 A streptavidin variant with slower biotin dissociation and increased mechanostability Chivers, Claire E. Crozat, Estelle Chu, Calvin Moy, Vincent T. Sherratt, David J. Howarth, Mark Nat Methods Article Streptavidin binds biotin-conjugates with exceptional stability, but dissociation does occur and can be limiting in imaging, DNA amplification, and nanotechnology. We identified a mutant streptavidin, which we call traptavidin, showing ~10-fold slower biotin off-rate, increased mechanical strength, and improved thermostability; this resilience should find diverse applications. We show that the motor protein FtsK could strip proteins from DNA, rapidly displacing streptavidin from biotinylated DNA; traptavidin resisted displacement and thus indicated the force generated by FtsK translocation. 2010-04-11 2010-05 /pmc/articles/PMC2862113/ /pubmed/20383133 http://dx.doi.org/10.1038/nmeth.1450 Text en Users may view, print, copy, download and 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
Chivers, Claire E.
Crozat, Estelle
Chu, Calvin
Moy, Vincent T.
Sherratt, David J.
Howarth, Mark
A streptavidin variant with slower biotin dissociation and increased mechanostability
title A streptavidin variant with slower biotin dissociation and increased mechanostability
title_full A streptavidin variant with slower biotin dissociation and increased mechanostability
title_fullStr A streptavidin variant with slower biotin dissociation and increased mechanostability
title_full_unstemmed A streptavidin variant with slower biotin dissociation and increased mechanostability
title_short A streptavidin variant with slower biotin dissociation and increased mechanostability
title_sort streptavidin variant with slower biotin dissociation and increased mechanostability
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2862113/
https://www.ncbi.nlm.nih.gov/pubmed/20383133
http://dx.doi.org/10.1038/nmeth.1450
work_keys_str_mv AT chiversclairee astreptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT crozatestelle astreptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT chucalvin astreptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT moyvincentt astreptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT sherrattdavidj astreptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT howarthmark astreptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT chiversclairee streptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT crozatestelle streptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT chucalvin streptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT moyvincentt streptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT sherrattdavidj streptavidinvariantwithslowerbiotindissociationandincreasedmechanostability
AT howarthmark streptavidinvariantwithslowerbiotindissociationandincreasedmechanostability

Ejemplares similares