Biotin-assisted folding of streptavidin on the yeast surface

Biotechnology Progress

Volumn 28, Issue 1, 2012, Pages 276-283

  Hong Lim, Kok ^a   Hwang, Inseong ^b   Park, Sheldon ^a  

^a State University of New York   (United States)

^b Seoul National University   (South Korea)

Author keywords

Biotin; Molecular chaperone; Protein folding; Streptavidin; Yeast display

Indexed keywords

BIOTECHNOLOGY APPLICATIONS; BIOTIN; BIOTINYLATED ANTIBODIES; CELL WALLS; CO-EXPRESSION; FUNCTIONAL MOLECULES; HIGH AFFINITY; IMMUNOPRECIPITATES; MOLECULAR CHAPERONES; NON-COVALENT INTERACTION; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN INDUCTION; PROTEIN TARGETS; SMALL MOLECULES; SOLID SURFACE; STREPTAVIDIN; SURFACE DISPLAYS; YEAST DISPLAY;

BIOTECHNOLOGY; COENZYMES; MOLECULES; MONOMERS; PROTEIN FOLDING; YEAST;

PROTEINS;

BIOTIN; CHAPERONE; STREPTAVIDIN;

ANIMAL; ARTICLE; BIOTECHNOLOGY; BIOTINYLATION; CHEMISTRY; FLOW CYTOMETRY; IMMUNOPRECIPITATION; KINETICS; METABOLISM; METHODOLOGY; MOUSE; PROTEIN FOLDING; PROTEIN PROCESSING; SACCHAROMYCES CEREVISIAE;

ANIMALS; BIOTECHNOLOGY; BIOTIN; BIOTINYLATION; FLOW CYTOMETRY; IMMUNOPRECIPITATION; KINETICS; MICE; MOLECULAR CHAPERONES; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; SACCHAROMYCES CEREVISIAE; STREPTAVIDIN;

BACTERIA (MICROORGANISMS); SACCHAROMYCES CEREVISIAE;

EID: 84856564365     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.721     Document Type: Article

References (45)

1. Gai SA, Wittrup KD. Yeast surface display for protein engineering and characterization. Curr Opin Struct Biol. 2007; 17: 467-473.
2. Pepper LR, Cho YK, Boder ET, Shusta EV. A decade of yeast surface display technology: where are we now? Comb Chem High Throughput Screen. 2008; 11: 127-34.
3. Coughlan CM, Walker JL, Cochran JC, Wittrup KD, Brodsky JL. Degradation of mutated bovine pancreatic trypsin inhibitor in the yeast vacuole suggests post-endoplasmic reticulum protein quality control. J Biol Chem. 2004; 279: 15289-15297.
4. Boder ET, Midelfort KS, Wittrup KD. Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proc Natl Acad Sci USA. 2000; 97: 10701-10705.
5. Shusta EV, Holler PD, Kieke MC, Kranz DM, Wittrup KD. Directed evolution of a stable scaffold for T-cell receptor engineering. Nat Biotechnol. 2000; 18: 754-759.
6. Kieke MC, Shusta EV, Boder ET, Teyton L, Wittrup KD, Kranz DM. Selection of functional T cell receptor mutants from a yeast surface-display library. Proc Natl Acad Sci USA. 1999; 96: 5651-5656.
7. Starwalt SE, Masteller EL, Bluestone JA, Kranz DM. Directed evolution of a single-chain class II MHC product by yeast display. Protein Eng. 2003; 16: 147-156.
8. Esteban O, Zhao H. Directed evolution of soluble single-chain human class II MHC molecules. J Mol Biol. 2004; 340: 81-95.
9. Huang D, Shusta EV. Secretion and surface display of green fluorescent protein using the yeast Saccharomyces cerevisiae. Biotechnol Prog. 2005; 21: 349-357.
10. Kimura RH, Cheng Z, Gambhir SS, Cochran JR. Engineered knottin peptides: a new class of agents for imaging integrin expression in living subjects. Cancer Res. 2009; 69: 2435-2442.
11. Dutta S, Koide A, Koide S. High-throughput analysis of the protein sequence-stability landscape using a quantitative yeast surface two-hybrid system and fragment reconstitution. J Mol Biol. 2008; 382: 721-733.
12. Shiraga S, Ishiguro M, Fukami H, Nakao M, Ueda M. Creation of Rhizopus oryzae lipase having a unique oxyanion hole by combinatorial mutagenesis in the lid domain. Appl Microbiol Biotechnol. 2005; 68: 779-785.
13. Takayama K, Suye S, Kuroda K, Ueda M, Kitaguchi T, Tsuchiyama K, Fukuda T, Chen W, Mulchandani A. Surface display of organophosphorus hydrolase on Saccharomyces cerevisiae. Biotechnol Prog. 2006; 22: 939-943.
14. Breinig F, Diehl B, Rau S, Zimmer C, Schwab H, Schmitt MJ. Cell surface expression of bacterial esterase A by Saccharomyces cerevisiae and its enhancement by constitutive activation of the cellular unfolded protein response. Appl Environ Microbiol. 2006; 72: 7140-7147.
15. Kadonosono T, Kato M, Ueda M. Metallopeptidase, neurolysin, as a novel molecular tool for analysis of properties of cancer-producing matrix metalloproteinases-2 and -9. Appl Microbiol Biotechnol. 2007; 75: 1285-1291.
16. Sethuraman A, Belfort G. Protein structural perturbation and aggregation on homogeneous surfaces. Biophys J. 2005; 88: 1322-1333.
17. Billsten P, Freskgard PO, Carlsson U, Jonsson BH, Elwing H. Adsorption to silica nanoparticles of human carbonic anhydrase II and truncated forms induce a molten-globule-like structure. FEBS Lett. 1997; 402: 67-72.
18. Tsai SL, Oh J, Singh S, Chen RZ, Chen W. Functional assembly of minicellulosomes on the Saccharomyces cerevisiae cell surface for cellulose hydrolysis and ethanol production. Appl Environ Microbiol. 2009; 75: 6087-6093.
19. Tsai SL, Goyal G, Chen W. Surface display of a functional minicellulosome by intracellular complementation using a synthetic yeast consortium and its application to cellulose hydrolysis and ethanol production. Appl Environ Microbiol. 2010; 76: 7514-7520.
20. Wilchek M, Bayer EA. Foreword and introduction to the book (strept)avidin-biotin system. Biomol Eng. 1999; 16: 1-4.
21. Gonzalez M, Argarana CE, Fidelio GD. Extremely high thermal stability of streptavidin and avidin upon biotin binding. Biomol Eng. 1999; 16: 67-72.
22. Sano T, Cantor CR. Cooperative biotin binding by streptavidin. Electrophoretic behavior and subunit association of streptavidin in the presence of 6 M urea. J Biol Chem. 1990; 265: 3369-3373.
23. Rakestraw JA, Aird D, Aha PM, Baynes BM, Lipovsek D. Secretion-and-capture cell-surface display for selection of target-binding proteins. Protein Eng Des Sel. 2011; 24: 525-530.
24. Ali MH, Imperiali B. Protein oligomerization: how and why. Bioorg Med Chem. 2005; 13: 5013-5020.
25. Weaver-Feldhaus JM, Lou J, Coleman JR, Siegel RW, Marks JD, Feldhaus MJ. Yeast mating for combinatorial Fab library generation and surface display. FEBS Lett. 2004; 564: 24-34.
26. Boder ET, Bill JR, Nields AW, Marrack PC, Kappler JW. Yeast surface display of a noncovalent MHC class II heterodimer complexed with antigenic peptide. Biotechnol Bioeng. 2005; 92: 485-491.
27. Lim KH, Madabhushi SR, Mann J, Neelamegham S, Park S. Disulfide trapping of protein complexes on the yeast surface. Biotechnol Bioeng. 2010; 106: 27-41.
28. Gallizia A, de Lalla C, Nardone E, Santambrogio P, Brandazza A, Sidoli A, Arosio P. Production of a soluble and functional recombinant streptavidin in Escherichia coli. Protein Expr Purif. 1998; 14: 192-196.
29. Furukawa H, Tanino T, Fukuda H, Kondo A. Development of novel yeast cell surface display system for homo-oligomeric protein by coexpression of native and anchored subunits. Biotechnol Prog. 2006; 22: 994-997.
30. Sano T, Cantor CR. Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin. Proc Natl Acad Sci USA. 1995; 92: 3180-3184.
31. Chilkoti A, Tan PH, Stayton PS. Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120. Proc Natl Acad Sci USA. 1995; 92: 1754-1758.
32. Boder ET, Wittrup KD. Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol. 1997; 15: 553-557.
33. Clements JM, Catlin GH, Price MJ, Edwards RM. Secretion of human epidermal growth factor from Saccharomyces cerevisiae using synthetic leader sequences. Gene. 1991; 106: 267-271.
34. Wu SC, Wong SL. Engineering soluble monomeric streptavidin with reversible biotin binding capability. J Biol Chem. 2005; 280: 23225-23231.
35. Lim KH, Huang H, Pralle A, Park S. Engineered Streptavidin monomer and dimer with improved stability and function (DOI: 10.121/bi2010366).
36. Green NM. Avidin and streptavidin. Methods Enzymol. 1990; 184: 51-67.
37. Katz BA. Binding of biotin to streptavidin stabilizes intersubunit salt bridges between Asp61 and His87 at low pH. J Mol Biol. 1997; 274: 776-800.
38. Shibasaki S, Kawabata A, Ishii J, Yagi S, Kadonosono T, Kato M, Fukuda N, Kondo A, Ueda M. Construction of a novel synergistic system for production and recovery of secreted recombinant proteins by the cell surface engineering. Appl Microbiol Biotechnol. 2007; 75: 821-828.
39. Cho YK, Chen I, Wei X, Li L, Shusta EV. A yeast display immunoprecipitation method for efficient isolation and characterization of antigens. J Immunol Methods. 2009; 341: 117-126.
40. Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem. 2006; 75: 333-366.
41. Neef DW, Turski ML, Thiele DJ. Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol. 2010; 8: e1000291.
42. Tsaytler P, Harding HP, Ron D, Bertolotti A. Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science. 2011; 332: 91-94.
43. Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR. Structural origins of high-affinity biotin binding to streptavidin. Science. 1989; 243: 85-88.
44. Katchalski-Katzir E. Immobilized enzymes-learning from past successes and failures. Trends Biotechnol. 1993; 11: 471-478.
45. Mateo C, Palomo JM, Fernandez-Lorente, G, Guisan JM, Fernandez-Lafuente R. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb Technol. 2007; 40: 1451-1463.