Escherichia coli fusion carrier proteins act as solubilizing agents for recombinant uncoupling protein 1 through interactions with GroEL

Biochemical and Biophysical Research Communications

Volumn 333, Issue 3, 2005, Pages 686-693

  Douette, Pierre ^a   Navet, Rachel ^a   Gerkens, Pascal ^a   Galleni, Moreno ^a   Lévy, Daniel ^b   Sluse, Francis E ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b INSTITUT CURIE   (France)

Author keywords

Aggregation; Fusion protein; GroEL ES; Maltose binding protein; N utilizing substance A; Solubility; Uncoupling protein 1

Indexed keywords

CHAPERONIN; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; N UTILIZING SUBSTANCE A; POLYPEPTIDE; PROTEIN DERIVATIVE; RECOMBINANT PROTEIN; RECOMBINANT UNCOUPLING PROTEIN 1; SOLUBILIZER; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN 1;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ELECTRON MICROSCOPY; ESCHERICHIA COLI; GEL FILTRATION; HYDROPHOBICITY; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; SOLUBILITY; SOLUBILIZATION;

AMINO ACID SEQUENCE; CARRIER PROTEINS; CHROMATOGRAPHY, AFFINITY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; ION CHANNELS; MANNOSE-BINDING LECTIN; MEMBRANE PROTEINS; MITOCHONDRIAL PROTEINS; MOLECULAR SEQUENCE DATA; RECOMBINANT FUSION PROTEINS; SOLUBILITY;

ESCHERICHIA COLI; PROKARYOTA;

EID: 20744445059     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.05.164     Document Type: Article

References (27)

1. G. Georgiou, and P. Valax Expression of correctly folded proteins in Escherichia coli Curr. Opin. Biotechnol. 7 1996 190 197
2. F. Baneyx Recombinant protein expression in Escherichia coli Curr. Opin. Biotechnol. 10 1999 411 421
3. H.P. Sorensen, and K.K. Mortensen Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli Microb. Cell Factory 4 2005 1 8
4. A. Villaverde, and M.M. Carrio Protein aggregation in recombinant bacteria: biological role of inclusion bodies Biotechnol. Lett. 25 2003 1385 1395
5. A. Middelberg Preparative protein refolding Trends Biotechnol. 20 2002 437 443
6. R.B. Kapust, and D.S. Waugh Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Sci. 8 1999 1668 1674
7. V. De Marco, G. Stier, S. Blandin, and A. de Marco The solubility and stability of recombinant proteins are increased by their fusion to NusA Biochem. Biophys. Res. Commun. 322 2004 766 771
8. F.U. Hartl Molecular chaperones in cellular protein folding Nature 381 1996 571 579
9. F.U. Hartl, and M. Hayer-Hartl Molecular chaperones in the cytosol: from nascent chain to folded protein Science 295 2002 1852 1858
10. P. Goloubinoff, A.A. Gatenby, and G.H. Lorimer GroE heat shock proteins promote assembly of foreign prokaryotic ribulose biphosphate carboxylase oligomers in Escherichia coli Nature 337 1989 44 47
11. P. Douette, R. Navet, F. Bouillenne, A. Brans, C. Sluse-Goffart, A. Matagne, and F.E. Sluse Secondary-structure characterization by far-UV CD of highly purified uncoupling protein1 expressed in yeast Biochem. J. 380 2004 139 145
12. M. Klingenberg, and K.S. Echtay Uncoupling proteins: the issues from a biochemist point of view Biochim. Biophys. Acta 1504 2001 128 143
13. K.S. Echtay, E. Winkler, and M. Klingenberg Coenzyme Q is an obligatory cofactor for uncoupling protein function Nature 408 2000 609 613
14. R. Marabini, I.M. Masegosa, C. San Martìn, S. Marco, J.J. Fernández, L.G. de la Fraga, C. Vaquerizo, and J.M. Carazo Xmipp: an image processing package for electron microscopy J. Struct. Biol. 116 1996 237 240
15. S. Marco, M. Chagoyen, L.G. de la Fraga, J.M. Carazo, and J.L. Carrascosa A variant to the random approximation of the reference-free alignment algorithm Ultramicroscopy 66 1996 5 10
16. K. Braig, Z. Otwinowski, R. Hegde, D.C. Boisvert, A. Joachimiak, A.L. Horwich, and P.B. Sigler The crystal structure of the bacterial chaperonin GroEL at 2.8 Å Nature 371 1994 578 586
17. O. Llorca, S. Marco, J.L. Carrascosa, and J.M. Valpuesta Conformational changes in the GroEL oligomer during the functional cycle J. Struct. Biol. 118 1997 31 42
18. H. Taguchi, and M. Yoshida Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin FEBS Lett. 359 1995 195 198
19. A. Richardson, S.J. Landry, and G. Georgopoulos The ins and outs of a molecular chaperone machine Trends Biochem. Sci. 23 1998 138 143
20. W.A. Houry, D. Frishman, C. Eckerckorn, F. Lottspeich, and F.U. Hartl Identification of in vivo substrates if the chaperonin GroEL Nature 402 1999 147 154
21. G. Richarme, and T.D. Caldas Chaperone properties of the bacterial periplasmic substrate-binding proteins J. Biol. Chem. 272 1997 15607 15612
22. H. Lilie, K. Lang, R. Rudolph, and J. Buchner Prolyl isomerases catalyze antibody folding in vitro Protein Sci. 2 1993 1490 1496
23. J.D. Fox, K.M. Routzahn, M.H. Bucher, and D.S. Waugh Maltodextrin-binding proteins from diverse bacteria and archae are potent solubility enhancers FEBS Lett. 537 2003 53 57
24. Y.-S. Huang, and D.T. Chuang Mechanisms for GroEL/GroES-mediated folding of a large 86-kDa fusion polypeptide in vitro J. Biol. Chem. 274 1999 10405 10412
25. J.C. Spurlino, G.-Y. Lu, and F.A. Quiocho The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis J. Biol. Chem. 266 1991 5202 5219
26. J.D. Fox, R.B. Kapust, and D.S. Waugh Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins Protein Sci. 10 2001 622 630
27. D. Sachdev, and J.M. Chirgwin Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli Biochem. Biophys. Res. Commun. 244 1998 933 937