Chaperone-assisted protein expression

Structure

Volumn 4, Issue 3, 1996, Pages 239-242

  Cole, Philip A ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN;

ARTICLE; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENETIC RECOMBINATION; GENETICS; METABOLISM; PLASMID; PROTEIN FOLDING; PROTEIN PROCESSING;

ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GROEL PROTEIN; GROES PROTEIN; MOLECULAR CHAPERONES; PLASMIDS; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINATION, GENETIC;

ESCHERICHIA COLI;

EID: 0030584654     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00028-7     Document Type: Article

References (29)

1. Studier, F.W., Rosenberg, A.H., Dunn, JJ. & Dubendorf, J.W. (1990). Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
2. Carrera, A.C., Alexandrov, K. & Roberts, T.M. (1993). The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP. Proc. Natl. Acad. Sci. USA 90, 442-446.
3. Noel, J.P., et al., & Tsai, M.D. (1991). Phospholipase A2 engineering. X-ray structural and functional evidence for the interaction of lysine-56 with substrates. Biochemistry 30, 11801 -11811.
4. Gaitanaris, G.A., Vysokanov, A., Hung, S.C., Gottesman, M.E. & Gragerov, A. (1994). Successive action of Escherichia coli chaperones in vivo. Molecular Microbiology 14, 861-869.
5. Georgopoulos, C.P., Hendrix, R.W., Casjens, S.R. & Kaiser, A.D. (1973). Host participation in bacteriophage lambda head assembly. J. Mol. Biol. 76, 45-60.
6. Goloubinoff, P., Gatenby, A.A. & Lorimer, G.H. (1989). GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 337, 44-47.
7. Cheng, M.Y., et al., & Horwich, A.L. (1989). Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337, 620-625.
8. Braig, K., et al., & Sigler, P.B. (1994). The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371, 578-586.
9. Hendrix, R.W. (1979). Purification and properties of groE, a host protein involved in bacteriophage assembly. J. Mol. Biol. 129, 375-392.
10. Hayer-Hartl, M.K., Martin, J. & Hartl, F.U. (1995). Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Science 269, 836-841.
11. Bougeret, C., Rothhut, B., Pascale, J., Fischer, S. & Benarous, R. (1993). Recombinant Csk expressed in Escherichia coli is autophosphorylated on tyrosine residue(s). Oncogene 8, 1241-1247.
12. Caspers, P., Stieger, M. & Burn, P. (1994). Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases in E. coli. Cell. Mol. Biol. 40, 635-644.
13. Amrein, K.E., et al., & Burn, P. (1995). Purification and characterization of human recombinant p50csk protein tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL Proc. Natl. Acad. Sci. USA. 92, 1048-1052.
14. Cole, P.A., Burn, P., Takacs, B. & Walsh, C.T. (1994). Evaluation of the catalytic mechanism of recombinant human Csk (C-terminal Src kinase) using nucleotide analogs and viscosity effects. J. Biol. Chem. 269, 30880-30887.
15. Koegel, M., Kypta, R.M., Bergman, M., Alitalo, K. & Courtneidge (1994). Rapid and efficient purification of Src homology 2 domain-containing proteins: Fyn, Csk and phosphatidylinositol 3-kinase p85. Biochem. J. 302, 737-744.
16. Cole, P.A., Grace, M.R., Phillips, R.S., Burn, P. & Walsh, C.T. (1995). The role of the catalytic base in the protein tyrosine kinase Csk. J. Biol. Chem. 270, 22105-22108.
17. Dale, G.E., Schonfeld, H.-J., Langen, H. & Stieger, M. (1994). Increased solubility of trimethoprim-resistant type S1 DHFR from Staphylococcus aureus in Escherichia coli cells overproducing the chaperonins GroEL and GroES. Protein Eng. 7, 925-931.
18. Davie, J.R., et al., & Lau, K.S. (1995). Expression and characterization of branched-chain α-ketoacid dehydrogenase kinase from the rat. J. Biol. Chem. 270, 19861-19867.
19. Zhi, W., Landry, S.J., Gierasch, L.M. & Srere, P.A. (1992). Renaturation of citrate synthase: influence of denaturant and folding assistants. Protein Sci. 1, 522-529.
20. Badcoe, I.G., et al., & Clarke, A.R. (1991). Binding of a chaperonin to the folding intermediates of lactate dehydrogenase Biochemistry 30, 9195-9200.
21. Mizobata, T., Akiyama, Y., Ito, K., Yumoto, N. & Kawata, Y. (1992). Effects of the Chaperonin GroE on the refolding of tryptophanase from Escherichia coli. J. Biol. Chem. 267, 17773-17779.
22. Zheng, X., Rosenberg, L.E., Kalousek, F. & Fenton, W. A. (1993). GroEL, GroES, and ATP-dependent folding and spontaneous assembly of ornithine transcarbamylase. J. Biol. Chem. 268, 7489-7493.
23. Laminet, A.A., Ziegelhoffer, T., Georgopoulos, C. & Pluckthun, A. (1990). The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor. EMBO J. 9, 2315-2319.
24. Mendoza, J.A., Rogers, E., Lorimer, G.H. & Horowitz, P.M. (1991). Chaperonins facilitate the in vitro folding of monomeric rhodanese. J. Biol. Chem. 266, 13044-13049.
25. Goloubinoff, P., Christeller, J.T., Gatenby, A.A. & Lorimer, G.H. (1989). Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 342, 884-889.
26. Wynn, R.M., Davie, J.R., Cox, R.P. & Chuang, D.T. (1992). Chaperonins GroEL and GroES promote assembly of heterotetramers (α2β2) of mammalian mitochondrial branched-chain α-keto acid decarboxylase in Escherichia coli. J. Biol. Chem. 267, 12400-12403.
27. Roman, L.J., Sheta, E.A., Martasek, P., Gross, S.S., Liu, Q. & Masters, B.S. (1995). High-level expression of functional rat neuronal nitric oxide synthase in Escherichia coli. Proc. Natl. Acad. Sci. USA 92, 8428-8432.
28. Perez-Perez, J., Martinez-Caja, C., Barbero, J.L. & Gutierrez, J. (1995). DnaK/DnaJ supplementation improves the periplasmic production of human granulocyte-colon stimulating factor in Escherichia coli. Biochem. Biophys. Res. Commun. 210, 524-529.
29. Blum, P., Velligan, M., Lin, N. & Matin, A. (1992). DnaK-mediated alterations in human growth hormone protein inclusion bodies. Biotechnology 10, 301-304.