Formation of fluorescent proteins by the attachment of phycoerythrobilin to R-phycoerythrin alpha and beta apo-subunits

Analytical Biochemistry

Volumn 358, Issue 1, 2006, Pages 38-50

  Isailovic, Dragan ^a   Sultana, Ishrat ^a   Phillips, Gregory J ^a   Yeung, Edward S ^a  

^a IOWA STATE UNIVERSITY   (United States)

Author keywords

Bacteria; Fluorescence; Protein expression

Indexed keywords

ALGAE; BACTERIA; CELLS; CHROMOPHORES; CLONING; CYTOLOGY; ESCHERICHIA COLI; FLOW CYTOMETRY; FLUORESCENCE MICROSCOPY; RECOMBINANT PROTEINS;

CYTOTOXIC EFFECTS; DIFFERENTIAL INTERFERENCE CONTRAST MICROSCOPY; FLUORESCENT PROBES; FLUORESCENT PROTEIN; FLUORESCENT REPORTER; MALTOSE BINDING PROTEINS; PHYCOERYTHROBILIN; PROTEIN EXPRESSIONS;

FLUORESCENCE;

HISTIDINE; HYBRID PROTEIN; MALTOSE; PHYCOERYTHRIN; PROTEIN; PROTEIN SUBUNIT; UROBILIN;

ANIMAL CELL; ARTICLE; BACTERIAL CELL; CELL ADHESION; CELL INCLUSION; CHROMATOPHORE; CYTOTOXICITY; ESCHERICHIA COLI; FLOW CYTOMETRY; FLUORESCENCE; FLUORESCENCE MICROSCOPY; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RED ALGA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; RHODOPHYTA;

EID: 33749438752     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.08.011     Document Type: Article

References (34)

1. Lakowicz J.R. Principles of Fluorescence Spectroscopy (1999), Plenum Press, New York
2. Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67 (1998) 509-544
3. Zhang J., Campbell R.E., Thing A.Y., and Tsien R.Y. Creating new fluorescent probes for cell biology. Nat. Rev. Mol. Cell Biol. 3 (2002) 906-918
4. Glazer A.N., and Stryer L. Phycofluor probes. Trends Biochem. Soc. 9 (1984) 423-427
5. Mullins J.M. Phycobilliproteins. In: Javois L.C. (Ed). Immunocytochemical Methods and Protocols. Methods in Molecular Biology 34 (1994), Humana Press, Totowa, NJ 112-113
6. Zickendraht-Wendelstadt B., Friedrich J., and Rudiger W. Spectral characterization of monomeric C-phycoerythrin from Pseudanabaena W 1173 and its α and β subunits: Energy transfer in isolated subunits and C-phycoerythrin. Photochem. Photobiol. 31 (1980) 367-376
7. Isailovic D., Li H.-W., and Yeung E.S. Isolation and characterization of R-phycoerythrin subunits and enzymatic digests. J. Chromatogr. A 1051 (2004) 119-130
8. Tooley A.J., Cai Y.A., and Glazer A.N. Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-α subunit in a heterologous host. Proc. Natl. Acad. Sci. USA 98 (2001) 10560-10565
9. Tooley A.J., and Glazer A.N. Biosynthesis of the cyanobacterial light-harvesting polypeptide phycoerythrocyanin holo-α subunit in a heterologous host. J. Bacteriol. 184 (2002) 4666-4671
10. Cai Y.A., Murphy J.T., Wedemayer G.J., and Glazer A.N. Recombinant phycobiliproteins. Anal. Biochem. 290 (2001) 186-204
11. Beale S.I., and Cornejo J. Biosynthesis of phycobilins: Ferredoxin-mediated reduction of biliverdin catalyzed by extracts of Cyanidium caldarium. J. Biol. Chem. 266 (1991) 22328-22332
12. Beale S.I., and Cornejo J. Biosynthesis of phycobilins: 3(Z)-Phycoerythrobilin and 3(Z)-phycocyanobilin are intermediates in the formation of 3(E)-phycocyanobilin from biliverdin IXa. J. Biol. Chem. 266 (1991) 22333-22340
13. Beale S.I., and Cornejo J. Biosynthesis of phycobilins: 15,16-dihydrobiliverdin IXa is a partially reduced intermediate in the formation of phycobilins from biliverdin IXa. J. Biol. Chem. 266 (1991) 22341-22345
14. Schluchter M.W., and Glazer A.N. Biosynthesis of phycobiliproteins in cyanobacteria. In: Peschek G.A., Löffelhardt W., and Schmetterer G. (Eds). The Phototrophic Prokaryotes (1999), Kluwer Academic/Plenum, New York 83-95
15. 1-Cys-α84-phycoviolobilin chromophore of phycoerythrocyanin. Biochemistry 40 (2001) 12444-12456
16. Arciero D.M., Bryant D.A., and Glazer A.N. In vitro attachment of bilins to apophycocyanin I. Specific covalent adduct formation at cysteinyl residues involved in phycocyanobilin binding in C-phycocyanin. J. Biol. Chem. 263 (1988) 18343-18349
17. Arciero D.M., Dallas J.L., and Glazer A.N. In vitro attachment of bilins to apophycocyanin II. Determination of the structures of tryptic bilin peptides derived from the phycocyanobilin adduct. J. Biol. Chem. 263 (1988) 18350-18357
18. Arciero D.M., Dallas J.L., and Glazer A.N. In vitro attachment of bilins to apophycocyanin III. Properties of the phycoerythrobilin adduct. J. Biol. Chem. 263 (1988) 18358-18363
19. Fairchild C.D., and Glazer A.N. Nonenzymatic bilin addition to the α subunit of an apophycoerythrin. J. Biol. Chem. 269 (1994) 28988-28996
20. Murphy J.T., and Lagarias J.C. The phytofluors: A new class of fluorescent protein probes. Curr. Biol. 7 (1997) 870-876
21. Kahn K., Mazel D., Houmard J., Tandeau de Marsac N., and Schaefer M.R. A role for cpeYZ in cyanobacterial phycoerythrin biosynthesis. J. Bacteriol. 179 (1997) 998-1006
22. Roell M.K., and Morse D.E. Organization, expression, and nucleotide sequence of the operon encoding R-phycoerythrin α and β subunits from the red alga Polysiphonia boldii. Plant Mol. Biol. 21 (1993) 47-58
23. Isailovic D., Li H.-W., Phillips G.J., and Yeung E.S. High-throughput single-cell fluorescence spectroscopy. Appl. Spectrosc. 59 (2005) 221-226
24. Mitraki A., and King J. Protein folding intermediates and inclusion body formation. Biotechnology 7 (1989) 690-697
25. Kane J.F., and Hartley D.L. Formation of recombinant protein inclusion bodies in Escherichia coli. Trends Biotechnol. 6 (1988) 95-101
26. Villaverde A., and Carrió M.M. Protein aggregation in recombinant bacteria: Biological role of inclusion bodies. Biotechnol. Lett. 25 (2003) 1385-1395
27. Wedemayer G.J., Kidd D.G., Wemmer D.E., and Glazer A.N. Phycobilins of cryptophycean algae: Occurrence of dihydrobiliverdin and mesobiliverdin in cryptomonad biliproteins. J. Biol. Chem. 267 (1992) 7315-7331
28. Bowden G.A., Paredes A.M., and Georgiou G. Structure and morphology of protein inclusion bodies in Escherichia coli. Biotechnology 9 (1991) 725-730
29. Sriubolmas N., Panbangred W., Sriurairatana S., and Meevootisom V. Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase. Appl. Microbiol. Biotechnol. 47 (1997) 373-378
30. Carrió M.M., Corchero J.L., and Villaverde A. Dynamics of in vivo protein aggregation: Building inclusion bodies in recombinant bacteria. FEMS Microbiol. Lett. 169 (1998) 9-15
31. Pierce Biotechnology, Inclusion body solubilization reagent, 2003-2004, in: Applications Handbook and Catalog, Pierce Biotechnology, Rockford, IL, p. 162.
32. Thomas J.D., Daniel R.A., Errington J., and Robinson C. Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Mol. Microbiol. 39 (2001) 47-53
33. Feilmeier B.J., Iseminger G., Schroeder D., Webber H., and Phillips G.J. Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J. Bacteriol. 182 (2000) 4068-4076
34. Huang B., Wang G.-C., Zeng C.-K., and Li Z.-G. The experimental research of R-phycoerythrin subunits on cancer treatment: A new photosensitizer in PDT. Cancer Biother. Radiopharm. 17 (2002) 35-42