Abstract
The wide application of magnetic bead technology has been greatly facilitated by the use of streptavidin (avidin)-biotin systems, with which a variety of biological materials can be tightly immobilized on solid surfaces. The streptavidin gene was cloned from Streptomyces avidinii, and it was expressed at high levels in Escherichia coli despite potent antibacterial action of the gene product. The DNA sequence has been modified to provide streptavidin with a number of basic variations in size, stability, and biotin-binding characteristics, and to construct a system that allows the design of multi-functional proteins by making novel gene fusions with the streptavidin gene. These genetically engineered streptavidins are extremely useful for a variety of biotechnological applications, including those with magnetic beads.
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References
Chaiet L, Miller TW, Tausing F, and Wolf FJ (1963). Antibiotic MSD-235. II. Separation and purification of synergistic components. Antimicrob. Agents Chemother. 3, 28–32.
Chalet L and Wolf FJ (1964). The properties of streptavidin, a biotin-binding protein produced by Streptomycetes. Arch. Biochem. Biophys. 106, 1–5.
Green NM (1970). Avidin. Adv. Prot. Chem.29, 85–133.
Green NM (1990). Avidin and streptavidin. Methods Enzymol. 184, 51–60.
Argarada CE, Kuntz ID, Birken S, Axel R, and Cantor CR (1986). Molecular cloning and nucleotide sequence of the streptavidin gene.Nucleic Acids Res. 14, 1871–1882.
Cronan JE Jr (1990). Biotination of protein in vivo. A post-translational modification to label, purify, and study proteins.J. Biol. Chem. 265, 10327–10333.
Sano T and Cantor CR (1990). Expression of a cloned streptavidin gene inEscherichia coli. Proc. Natl. Acad. Sci. USA87, 142–146.
Studier FW, Rosenberg AH, Dunn JJ, and Dubendorf JW (1990). Use of T7 RNA polymerase to direct expression of cloned genes.Methods Enzymol. 185, 60–89.
Moffatt BA and Studier FW (1987). T7 lysozyme inhibits transcription by T7 RNA polymerase.Cell 49, 221–227.
Hoffman K, Wood SW, Brinton CC, Montibeller JA, and Finn FM (1980). Iminobiotin affinity columns and their application to retrieval of streptavidin.Proc. Natl. Acad. Sci. USA 77, 4666–4668.
Hendrickson WA, Pähler A, Smith JL, Satow Y, Merritt EA, and Phizackerley RP (1989). Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation.Proc. Natl. Acad. Sci. USA 86, 2190–2194.
Weber PC, Ohlendorf DH, Wendoroski JJ, and Salemme FR (1989). Structural origin of high affinity biotin binding to streptavidin.Science 243, 85–88.
Sano T, Pandori MW, Chen X, Smith CL, and Cantor CR (1995). Recombinant core streptavidin. A minimum-sized core streptavidin has enhanced structural stability and higher accessibility to biotinylated macromolecules.J. Biol. Chem. 270, 28204–28209.
Sano T and Cantor CR (1995). Inter-subunit contacts made by tryptophan-120 are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin.Proc. Natl. Acad. Sci. USA 92, 3180–3184.
Reznik GO, Vajda S, Smith CL, Cantor CR, and Sano T (1996). Streptavidins with intersubunit crosslinks have enhanced stability.Nature Biotechnol. 14, 1007–1011.
Sano T, Vajda S, Smith CL, and Cantor CR (1997). Engineering subunit association of multi-subunit proteins: A dimeric streptavidin. Submitted for publication.
Sano T, Smith CL, and Cantor CR (1993). A streptavidin mutant containing a cysteine stretch that facilitates production of a variety of specific streptavidin conjugates.Bio/Technology 11, 201–206.
Sano T and Cantor CR (1991). A streptavidin protein A chimera that allows one-step production of a variety of specific antibody conjugates.Bio/Technology 9, 1378–1381.
Sano T, Smith CL, and Cantor CR (1992). Immuno-PCR: Very sensitive antigen detection by means ofspecific antibody-DNA conjugates.Science 258, 120–122.
Sano T, Glazer AN, and Cantor CR (1992). A streptavidin-metallothionein chimera that allows specific labeling of biological materials with many different heavy metal ions.Proc. Natl. Acad. Sci. USA 89, 1534–1538.
Miyamoto S and Kollman PA (1993). Absolute and relative binding free energy calculations of the interaction of biotin and its analogs with streptavidin using molecular dynamics/free energy perturbation approaches.Proteins: Struct. Function Gent. 16, 226–245.
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Sano, T., Reznik, G., Vajda, S., Cantor, C.R., Smith, C.L. (1997). Properties and Applications of Genetically Engineered Streptavidins. In: Häfeli, U., Schütt, W., Teller, J., Zborowski, M. (eds) Scientific and Clinical Applications of Magnetic Carriers. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-6482-6_21
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DOI: https://doi.org/10.1007/978-1-4757-6482-6_21
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