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

102 Citations (Scopus)

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 languageEnglish
Pages (from-to)391-393
Number of pages3
JournalNature Methods
Volume7
Issue number5
DOIs
StatePublished - May 1 2010
Externally publishedYes

Fingerprint

Streptavidin
Biotin
Chromosome Segregation
Nanotechnology
DNA
Chromosomes
Strength of materials
Amplification
Imaging techniques
Proteins
traptavidin

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology
  • Biochemistry
  • Cell Biology

Cite this

Chivers, C. E., Crozat, E., Chu, C., Moy, V. T., Sherratt, D. J., & Howarth, M. (2010). A streptavidin variant with slower biotin dissociation and increased mechanostability. Nature Methods, 7(5), 391-393. https://doi.org/10.1038/nmeth.1450

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.

In: Nature Methods, Vol. 7, No. 5, 01.05.2010, p. 391-393.

Research output: Contribution to journal › Article

Chivers, CE, Crozat, E, Chu, C, Moy, VT, Sherratt, DJ & Howarth, M 2010, 'A streptavidin variant with slower biotin dissociation and increased mechanostability', Nature Methods, vol. 7, no. 5, pp. 391-393. https://doi.org/10.1038/nmeth.1450
Chivers CE, Crozat E, Chu C, Moy VT, Sherratt DJ, Howarth M. A streptavidin variant with slower biotin dissociation and increased mechanostability. Nature Methods. 2010 May 1;7(5):391-393. https://doi.org/10.1038/nmeth.1450
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. In: Nature Methods. 2010 ; Vol. 7, No. 5. pp. 391-393.
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