Tamavidin 2-REV: An engineered tamavidin with reversible biotin-binding capability

Journal of Biotechnology

Volumn 164, Issue 1, 2013, Pages 19-25

  Takakura, Yoshimitsu ^a   Sofuku, Kozue ^a   Tsunashima, Masako ^a  

^a JAPAN TOBACCO INC   (Japan)

Author keywords

Affinity purification; Avidin; Biotinylated protein; Reversible biotin binding; Tamavidin

Indexed keywords

AFFINITY PURIFICATION; AVIDIN; BIOTIN BINDING; BOVINE SERUM ALBUMINS; GENETICALLY MODIFIED; HIGH LEVEL EXPRESSION; ISO-ELECTRIC POINTS; TAMAVIDIN;

AFFINITY CHROMATOGRAPHY; AMINO ACIDS; ESCHERICHIA COLI; GLYCOPROTEINS; HYDROGEN BONDS; PROTEINS; PURIFICATION;

COENZYMES;

AGAROSE; ALANINE; BINDING PROTEIN; BIOTIN; FUNGAL PROTEIN; HYDROGEN; SULFATRIAD; TAMAVIDIN 2; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ARTICLE; BINDING AFFINITY; BIOENGINEERING; BIOTINYLATION; CONTROLLED STUDY; COVALENT BOND; ESCHERICHIA COLI; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN STRUCTURE;

ALANINE; AMINO ACID SUBSTITUTION; ANIMALS; AVIDIN; BIOTIN; CARRIER PROTEINS; CATTLE; ESCHERICHIA COLI; FUNGAL PROTEINS; IMMOBILIZED PROTEINS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STABILITY; RECOMBINANT PROTEINS; SERINE; SERUM ALBUMIN, BOVINE;

BOVINAE; ESCHERICHIA COLI;

EID: 84875090231     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.01.006     Document Type: Article

References (21)

1. Chilkoti A., Tan P.H., Stayton P.S. Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120. Proceedings of the National Academy of Sciences of the United States of America 1995, 92:1754-1758.
2. Green N.M. Avidin and streptavidin. Methods in Enzymology 1990, 184:51-67.
3. Hyre D.E., Le Trong I., Freitag S., Stenkamp R.E., Stayton P.S. Ser45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin system. Protein Science 2000, 9:878-885.
4. Hyre D.E., Le Trong I., Merritt E.A., Eccleston J.F., Green N.M., Stenkamp R.E., Stayton P.S. Cooperative hydrogen bond interactions in the streptavidin-biotin system. Protein Science 2006, 15:459-467.
5. Kopetzki, E., Muller, R., Engh, R., Schmitt, U., Deger, A., Brandstetter, H., inventors; Roche Diagnostics GmbH, assignee, 1997 October 8. Recombinant inactive core streptavidin mutants. European Patent 0799890 B1.
6. Laitinen O.H., Hytönen V.P., Nordlund H.R., Kulomaa M.S. Genetically engineered avidins and streptavidins. Cellular and Molecular Life Sciences 2006, 63:2992-3017.
7. Laitinen O.H., Airenne K.J., Marttila A.T., Kulik T., Porkka E., Bayer E.A., Wilchek M., Kulomaa M.S. Mutation of a critical tryptophan to lysine in avidin or streptavidin may explain why sea urchin fibropellin adopts an avidin-like domain. FEBS Letters 1999, 461:52-58.
8. Laitinen O.H., Nordlund H.R., Hytönen V.P., Uotila S.T., Marttila A.T., Savolainen J., Airenne K.J., Livnah O., Bayer E.A., Wilchek M., Kulomaa M.S. Rational design of an active avidin monomer. Journal of Biological Chemistry 2003, 278:4010-4014.
9. Malmstadt N., Hyre D.E., Ding Z., Hoffman A.S., Stayton P.S. Affinity thermoprecipitation and recovery of biotinylated biomolecules via a mutant streptavidin-smart polymer conjugate. Bioconjugate Chemistry 2003, 14:575-580.
10. Marttila A.T., Laitinen O.H., Airenne K.J., Kulik T., Bayer E.A., Wilchek M., Kulomaa M.S. Recombinant neutralite avidin: a non-glycosylated, acidic mutant of chicken avidin that exhibits high affinity for biotin and low non-specific binding properties. FEBS Letters 2000, 467:31-36.
11. Morag E., Bayer E.A., Wilchek M. Reversibility of biotin-binding by selective modification of tyrosine in avidin. Biochemical Journal 1996, 316:193-199.
12. O'Sullivan V.J., Barrette-Ng I., Hommema E., Hermanson G.T., Schofield M., Wu S.C., Honetschlaeger C., Ng K.S., Wong S.L. Development of a tetrameric streptavidin mutein with reversible biotin binding capability: engineering a mobile loop as an exit door for biotin. PLoS ONE 2012, 7:e35203.
13. Qureshi M.H., Wong S.L. Design, production, and characterization of a monomeric streptavidin and its application for affinity purification of biotinylated proteins. Protein Expression and Purification 2002, 25:409-415.
14. Qureshi M.H., Yeung J.C., Wu S.C., Wong S.L. Development and characterization of a series of soluble tetrameric and monomeric streptavidin muteins with differential biotin binding affinities. Journal of Biological Chemistry 2001, 276:46422-46428.
15. Sambrook J., Russell D.W. Molecular Cloning: A Laboratory Manual 2001, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 3rd ed.
16. Sano T., Cantor C.R. Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin. Proceedings of the National Academy of Sciences of the United States of America 1995, 92:3180-3184.
17. Schetters H. Avidin and streptavidin in clinical diagnosis. Biomolecular Engineering 1999, 16:73-78.
18. Takakura Y., Tsunashima M., Suzuki J., Usami S., Kakuta Y., Okino N., Ito M., Yamamoto T. Tamavidins - novel avidin-like biotin-binding proteins from the Tamogitake mushroom. FEBS Journal 2009, 276:1383-1397.
19. Wilchek M., Bayer E.A. Introduction to avidin-biotin technology. Methods in Enzymology 1990, 184:5-13.
20. Wu S.C., Wong S.L. Engineering soluble monomeric streptavidin with reversible biotin binding capability. Journal of Biological Chemistry 2005, 280:23225-23231.
21. Wu S.C., Wong S.L. Intracellular production of a soluble and functional monomeric streptavidin in Escherichia coli and its application for affinity purification of biotinylated proteins. Protein Expression and Purification 2006, 46:268-273.