In vivo self-assembly of fluorescent protein microparticles displaying specific binding domains

Bioconjugate Chemistry

Volumn 24, Issue 8, 2013, Pages 1314-1323

  Jahns, Anika C ^a,c   Maspolim, Yogananda ^a,d   Chen, Shuxiong ^a   Guthrie, Jenness M ^a   Blackwell, Len F ^a   Rehm, Bernd H A ^a,b  

^a MASSEY UNIVERSITY   (New Zealand)

^b MACDIARMID INSTITUTE FOR ADVANCED MATERIALS AND NANOTECHNOLOGY   (New Zealand)

^c UMEÅ UNIVERSITY   (Sweden)

^d NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; ESCHERICHIA COLI; FLUORESCENCE; RECOMBINANT PROTEINS;

BINDING DOMAIN; FLUORESCENT PROTEIN; IN-VIVO; MALTOSE BINDING PROTEINS; PROTEIN FUNCTIONALITIES; PROTEIN MICROPARTICLES; PROTEIN PARTICLES; RECOMBINANT ESCHERICHIA COLI; SELF-ASSEMBLE; SPECIFIC BINDING;

SELF ASSEMBLY;

AMINO ACID; FRUCTOSE BISPHOSPHATE ALDOLASE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; IMMUNOGLOBULIN G; MALTOSE BINDING PROTEIN; POLYESTER; PROTEIN A; PROTEIN G; PYROXYLIN; RESIN; SYNTHETASE; OLIGOPEPTIDE; PHOTOPROTEIN;

ARTICLE; BIOSEPARATION; CUPRIAVIDUS NECATOR; DENSITY GRADIENT; DNA SEQUENCE; DRY WEIGHT; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; GENE EXPRESSION; HUMAN; HYBRID GENE; IN VIVO STUDY; LIGAND BINDING; NONHUMAN; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN FUNCTION; SOLUBILITY; ULTRACENTRIFUGATION; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; PROCEDURES; PROTEIN ENGINEERING;

CUPRIAVIDUS NECATOR; ESCHERICHIA COLI;

CUPRIAVIDUS NECATOR; ESCHERICHIA COLI; LUMINESCENT PROTEINS; MODELS, MOLECULAR; OLIGOPEPTIDES; PROTEIN ENGINEERING; RECOMBINANT FUSION PROTEINS;

EID: 84883146235     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc300551j     Document Type: Article

References (47)

1. Shimomura, O., Johnson, F. H., and Saiga, Y. (1962) Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan Aequorea. J. Cell Comp. Physiol. 59, 223-239
2. Heim, R., Prasher, D. C., and Tsien, R. Y. (1994) Wavelength mutations and posttranslational autoxidation of green fluorescent protein Proc. Natl. Acad. Sci. U. S. A. 91, 12501-12504
3. Reid, B. G. and Flynn, G. C. (1997) Chromophore formation in green fluorescent protein Biochemistry 36, 6786-6791
4. Tsien, R. Y. (1998) The green fluorescent protein Annu. Rev. Biochem. 67, 509-544
5. Stuurman, N., Pacios Bras, C., Schlaman, H. R. M., Wijfjes, A. H. M., Bloemberg, G., and Spaink, H. P. (2000) Use of green fluorescent protein color variants expressed on stable broad-host-range vectors to visualize rhizobia interacting with plants Mol. Plant-Microbe Interact. 13, 1163-1169
6. Gurskaya, N. G., Fradkov, A. F., Terskikh, A., Matz, M. V., Labas, Y. A., Martynov, V. I., Yanushevich, Y. G., Lukyanov, K. A., and Lukyanov, S. A. (2001) GFP-like chromoproteins as a source of far-red fluorescent proteins FEBS Lett. 507, 16-20
7. de Groot, N. S. and Ventura, S. (2006) Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates J. Biotechnol. 125, 110-113
8. de Groot, N. S. and Ventura, S. (2006) Effect of temperature on protein quality in bacterial inclusion bodies FEBS Lett. 580, 6471-6476
9. Garcia-Fruitos, E., Gonzalez-Montalban, N., Morell, M., Vera, A., Ferraz, R. M., Aris, A., Ventura, S., and Villaverde, A. (2005) Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins Microb. Cell Fact 4, 27
10. Martinez-Alonso, M., Vera, A., and Villaverde, A. (2007) Role of the chaperone DnaK in protein solubility and conformational quality in inclusion body-forming Escherichia coli cells FEMS Microbiol. Lett. 273, 187-195
11. Martinez-Alonso, M., Garcia-Fruitos, E., and Villaverde, A. (2008) Yield, solubility and conformational quality of soluble proteins are not simultaneously favored in recombinant Escherichia coli Biotechnol. Bioeng. 101, 1353-1358
12. Martinez-Alonso, M., Gonzalez-Montalban, N., Garcia-Fruitos, E., and Villaverde, A. (2008) The functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum Appl. Environ. Microbiol. 174, 7431-7433
13. Garcia-Fruitos, E., Sabate, R., de Groot, N. S., Villaverde, A., and Ventura, S. (2011) Biological role of bacterial inclusion bodies: a model for amyloid aggregation FEBS J. 278, 2419-2427
14. Vera, A., Gonzalez-Montalban, N., Aris, A., and Villaverde, A. (2007) The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures Biotechnol. Bioeng. 96, 1101-1106
15. Peternel, S., Grdadolnik, J., Gaberc-Porekar, V., and Komel, R. (2008) Engineering inclusion bodies for non denaturing extraction of functional proteins Microbial Cell Factories 7, 34
16. Tsumoto, K., Umetsu, M., Kumagai, I., Ejima, D., and Arakawa, T. (2003) Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine Biochem. Biophys. Res. Commun. 312, 1383-1386
17. Rehm, B. H. A. (2006) Genetics and biochemistry of polyhydroxyalkanoate granule self-assembly: The key role of polyester synthases Biotechnol. Lett. 28, 207-213
18. Grage, K. and Rehm, B. H. A. (2008) In vivo production of scFv-displaying biopolymer beads using a self-assembly-promoting fusion partner Bioconjugate Chem. 19, 254-262
19. Jahns, A. C., Haverkamp, R. G., and Rehm, B. H. A. (2008) Multifunctional inorganic-binding beads self-assembled inside engineered bacteria Bioconjugate Chem. 19, 2072-2080
20. Brockelbank, J. A., Peters, V., and Rehm, B. H. A. (2006) Recombinant Escherichia coli strain produces a ZZ domain displaying biopolyester granules suitable for immunoglobulin G purification Appl. Environ. Microbiol. 72, 7394-7397
21. Grage, K., Jahns, A. C., Parlane, N., Palanisamy, R., Rasiah, I. A., Atwood, J. A., and Rehm, B. H. A. (2009) Bacterial polyhydroxyalkanoate granules: biogenesis, structure, and potential use as nano-/micro-beads in biotechnological and biomedical applications Biomacromolecules 10, 660-669
22. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular cloning: a laboratory manual, Cold Spring Harbor Laboratory Press, Plainview, NY.
23. Amara, A. A. and Rehm, B. H. A. (2003) Replacement of the catalytic nucleophile cysteine-296 by serine in class II polyhydroxyalkanoate synthase from Pseudomonas aeruginosa -mediated synthesis of a new polyester: identification of catalytic residues Biochem. J. 374, 413-421
24. Brandl, H., Gross, R. A., Lenz, R. W., and Fuller, R. C. (1988) Pseudomonas oleovorans as a source of poly(beta-hydroxyalkanoates) for potential applications as biodegradable polyesters Appl. Environ. Microbiol. 54, 1977-1982
25. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
26. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
27. Peters, V., Becher, D., and Rehm, B. H. A. (2007) The inherent property of polyhydroxyalkanoate synthase to form spherical PHA granules at the cell poles: the core region is required for polar localization J. Biotechnol. 132, 238-245
28. Mifune, J., Grage, K., and Rehm, B. H. A. (2009) Production of functionalized biopolyester granules by recombinant Lactococcus lactis Appl. Environ. Microbiol. 75, 4668-4675
29. Rehm, B. H. A. (2010) Bacterial polymers: biosynthesis, modifications and applications Nat. Rev. Microbiol. 8, 578-592
30. Rehm, B. H. A., Antonio, R. V., Spiekermann, P., Amara, A. A., and Steinbüchel, A. (2002) Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: in vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model Biochim. Biophys. Acta 1594, 178-190
31. Ringenberg, M., Lichtensteiger, C., and Vimr, E. (2001) Redirection of sialic acid metabolism in genetically engineered Escherichia coli Glycobiology 11, 533-539
32. Leffel, S. M., Mabon, S. A., and Stewart, C. N., Jr. (1997) Applications of green fluorescent protein in plants BioTechniques 23, 912-918
33. Phillips, G. N., Jr. (1997) Structure and dynamics of green fluorescent protein Curr. Opin. Struct. Biol. 7, 821-827
34. Naylor, L. H. (1999) Reporter gene technology: the future looks bright Biochem. Pharmacol. 58, 749-757
35. Misteli, T. and Spector, D. L. (1997) Applications of the green fluorescent protein in cell biology and biotechnology Nat. Biotechnol. 15, 961-964
36. Taylor, D. L., Woo, E. S., and Giuliano, K. A. (2001) Real-time molecular and cellular analysis: the new frontier of drug discovery Curr. Opin. Biotechnol. 12, 75-81
37. Atwood, J. A. and Rehm, B. H. A. (2009) Protein engineering towards biotechnological production of bifunctional polyester beads Biotechnol. Lett. 31, 131-137
38. Jahns, A. C. and Rehm, B. H. A. (2009) Tolerance of the Ralstonia eutropha class I polyhydroxyalkanoate synthase for translational fusions to its C terminus reveals a new mode of functional display Appl. Environ. Microbiol. 75, 5461-5466
39. Peters, V. and Rehm, B. H. A. (2005) In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases FEMS Microbiol. Lett. 248, 93-100
40. Peternel, S., Gaberc-Porekar, V., and Komel, R. (2009) Bacterial growth conditions affect quality of GFP expressed inside inclusion bodies Acta Chim. Slov. 56, 860-867
41. Vazquez, E., Cubarsi, R., Unzueta, U., Roldan, M., Domingo-Espin, J., Ferrer-Miralles, N., and Villaverde, A. (2010) Internalization and kinetics of nuclear migration of protein-only, arginine-rich nanoparticles Biomaterials 31, 9333-9339
42. Rehm, B. H. A. (2003) Polyester synthases: natural catalysts for plastics Biochem. J. 376, 15-33
43. Zhou, P., Lugovskoy, A. A., and Wagner, G. (2001) A solubility- enhancement tag (SET) for NMR studies of poorly behaving proteins J. Biomol. NMR 20, 11-14
44. Inouye, S. and Sahara, Y. (2008) Soluble protein expression in E. coli cells using IgG-binding domain of protein A as solubilizing partner in the cold induced system Biochem. Biophys. Res. Commun. 376, 448-453
45. Inouye, S. and Tsuji, F. I. (1994) Evidence for redox forms of the Aequorea green fluorescent protein FEBS Lett. 351, 211-214
46. Ward, W. W., Prentice, H. J., Roth, A. F., Cody, C. W., and Reeves, S. C. (1982) Spectral Perturbations of the Aequorea green-fluorescent protein Photochem. Photobiol. 35, 803-808
47. Fradkov, A. F., Verkhusha, V. V., Staroverov, D. B., Bulina, M. E., Yanushevich, Y. G., Martynov, V. I., Lukyanov, S., and Lukyanov, K. A. (2002) Far-red fluorescent tag for protein labelling Biochem. J. 368, 17-21