A streptavidin variant with slower biotin dissociation and increased mechanostability

Claire E. Chivers; Estelle Crozat; Calvin Chu; Vincent T. Moy; David J. Sherratt; Mark Howarth

doi:10.1038/nmeth.1450

A streptavidin variant with slower biotin dissociation and increased mechanostability

Claire E. Chivers, Estelle Crozat, Calvin Chu, Vincent T. Moy, David J. Sherratt, Mark Howarth

Research output: Contribution to journal › Article › peer-review

128 Scopus citations

Abstract

Streptavidin binds biotin conjugates with exceptional stability but dissociation does occur, limiting its use in imaging, DNA amplification and nanotechnology. We identified a mutant streptavidin, traptavidin, with more than tenfold slower biotin dissociation, increased mechanical strength and improved thermostability; this resilience should enable diverse applications. FtsK, a motor protein important in chromosome segregation, rapidly displaced streptavidin from biotinylated DNA, whereas traptavidin resisted displacement, indicating the force generated by Ftsk translocation.

Original language	English (US)
Pages (from-to)	391-393
Number of pages	3
Journal	Nature Methods
Volume	7
Issue number	5
DOIs	https://doi.org/10.1038/nmeth.1450
State	Published - May 2010
Externally published	Yes

ASJC Scopus subject areas

Biotechnology
Biochemistry
Molecular Biology
Cell Biology

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title = "A streptavidin variant with slower biotin dissociation and increased mechanostability",

abstract = "Streptavidin binds biotin conjugates with exceptional stability but dissociation does occur, limiting its use in imaging, DNA amplification and nanotechnology. We identified a mutant streptavidin, traptavidin, with more than tenfold slower biotin dissociation, increased mechanical strength and improved thermostability; this resilience should enable diverse applications. FtsK, a motor protein important in chromosome segregation, rapidly displaced streptavidin from biotinylated DNA, whereas traptavidin resisted displacement, indicating the force generated by Ftsk translocation.",

author = "Chivers, {Claire E.} and Estelle Crozat and Calvin Chu and Moy, {Vincent T.} and Sherratt, {David J.} and Mark Howarth",

note = "Funding Information: Funding was provided by the Wellcome Trust (M.H., D.J.S. and E.C.), the Biotechnology and Biological Sciences Research Council (C.E.C.), the US National Institutes of Health (V.T.M. and C.C.), the National Science Foundation (V.T.M.), the University of Miami (V.T.M.) and Worcester College Oxford (M.H.). We thank J.E. Graham and I. Grainge for helpful discussion.",

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AU - Chivers, Claire E.

AU - Crozat, Estelle

AU - Chu, Calvin

AU - Moy, Vincent T.

AU - Sherratt, David J.

AU - Howarth, Mark

N1 - Funding Information: Funding was provided by the Wellcome Trust (M.H., D.J.S. and E.C.), the Biotechnology and Biological Sciences Research Council (C.E.C.), the US National Institutes of Health (V.T.M. and C.C.), the National Science Foundation (V.T.M.), the University of Miami (V.T.M.) and Worcester College Oxford (M.H.). We thank J.E. Graham and I. Grainge for helpful discussion.

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AB - Streptavidin binds biotin conjugates with exceptional stability but dissociation does occur, limiting its use in imaging, DNA amplification and nanotechnology. We identified a mutant streptavidin, traptavidin, with more than tenfold slower biotin dissociation, increased mechanical strength and improved thermostability; this resilience should enable diverse applications. FtsK, a motor protein important in chromosome segregation, rapidly displaced streptavidin from biotinylated DNA, whereas traptavidin resisted displacement, indicating the force generated by Ftsk translocation.

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A streptavidin variant with slower biotin dissociation and increased mechanostability

Abstract

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