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 | |
| State | Published - May 1 2010 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biotechnology
- Biochemistry
- Molecular Biology
- Cell Biology
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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