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.

SUBMITTER: Chivers CE 

PROVIDER: S-EPMC2862113 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature