Genetic engineering of streptavidin, a versatile affinity tag.
Streptavidin, a tetrameric protein produced by Streptomyces avidinii, has been used as a useful, versatile affinity tag in a variety of biological applications. The efficacy of streptavidin is derived from its extremely high binding affinity for the vitamin biotin. For the last several years, we have used genetic engineering as a primary means to enhance the properties of streptavidin and to expand the application of streptavidin as an affinity tag. In this review, we describe several genetically engineered streptavidin variants, which include a streptavidin with a reduced biotin-binding affinity, a dimeric streptavidin, and a fusion protein between streptavidin and protein A, along with their potential applications in biological science.
Sano
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Center for Advanced Biotechnology and Department of Biomedical Engineering, Boston University, MA 02215, USA.
Vajda
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Cantor
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CR
D000345:Affinity Labels; D001710:Biotin / Q000378:metabolism; D003001:Cloning, Molecular; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013205:Staphylococcal Protein A / Q000235:genetics; D019809:Streptavidin / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
D000345:Affinity Labels; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A; D001710:Biotin; D019809:Streptavidin