A streptavidin variant with slower biotin dissociation and increased mechanostability.
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ABSTRACT:
SUBMITTER: Chivers CE
PROVIDER: S-EPMC2862113 | biostudies-literature | 2010 May
REPOSITORIES: biostudies-literature
Publications
A streptavidin variant with slower biotin dissociation and increased mechanostability.
Chivers Claire E CE Crozat Estelle E Chu Calvin C Moy Vincent T VT Sherratt David J DJ Howarth Mark M
Nature methods 20100411 5
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 trapta ...[more]
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