120
Views
10
CrossRef citations to date
0
Altmetric
Original Article

In vitro folding of a membrane protein: Effect of denaturation and renaturation on substrate binding by the lactose permease of Escherichia coli

&
Pages 15-20 | Received 08 Sep 1997, Accepted 22 Oct 1997, Published online: 09 Jul 2009

References

  • Kaback H. R. The lactose permease of Escherichla coli past, present and future. Handbook of Biological Physics: Transport Processes in Eukaryotic and Prokaryotic Organisms, W. N. Konings, H. R. Kaback, J. S. Lolkema. Elsevier, Amsterdam 1996; 203–227
  • Kaback H. R., Voss J., Wu J. Helix packing in polytopic membrane proteins: the lactose permease of Eschericvhia coli. Current Opinions in Structural Biology 1997; 7: 537–542
  • Jung H., Jung K., Kaback H. R. Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. I. Site-directed mutagenesis studies. Biochemistry 1994; 33: 12160–12165
  • Wu J., Kaback H. R. Cysteine 148 in the lactose permease {of Escherichia coli is a component of a substrate binding site. 2. Site-directed fluorescence studies. Biochemistry 1994; 33: 12166–12171
  • Frillingos S., Kaback H. R. Probing the conformation of the lactose permease of Escherichia coli by in situ site-directed sullfliydryl modification. Biochemistry 1996; 35: 3950–3956
  • Wu J., Fillingos S., Voss J., Kaback H. R. Ligand-induced conformation changes in the lactose permease of Escherichia coli: evidence for two binding sites. Protein Science 1994; 3: 2294–2301
  • Wickner W. The assembly of proteins into biological membranes: the membrane trigger hypothesis. Annual Review of Biochemistry 1979; 48: 23–45
  • Blobel G. Intracellular protein topogenesis. Proceedings National Academy Science USA 1980; 77: 1496–1500
  • Fiermonte G., Walker J. E., Palmieri F. Abundant bacterial expression and reconstitution of an intrinsic membrane-transport protein from bovine mitochondria. Biochemical Journal 1993; 294: 293–299
  • Rudolph R. Successful protein folding on an industrial scale. Protein Engineering. Principles and Practice, J. L. Cleland, C. S. Craik. Wiley-Liss, New York 1995; 283–298
  • Anfinsen C. B., Scheraga H. A. Experimental and theoretical aspects of protein folding. Advances Protein Chemistry 1975; 29: 205–300
  • Huang K. S., Bayley H., Liao M.-J., London E., Khorana H. G. Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacter-iorhodopsin and two proteolytic fragments. Journal of Biological Chemistry 1981; 256: 3802–3809
  • Dornmair K., Kiefer H., Jahnig F. Refolding of an integral membrane protein. OmpA of Escherichia coli. Journal of Biological Chemistry 1990; 31: 18907–18911
  • Surrey T., Schmid A., Jahnig F. Folding and membrane insertion of the trimeric beta-barrel protein OmpF. Biochemistry 1996; 35: 2283–2288
  • Surrey T., Jahnig F. Refolding and oriented insertion of a membrane protein into a lipid bilayer. Proceedings National Academy Science USA 1992; 89: 7457–7461
  • Wu J., Frillingos S., Kaback H. R. Dynamics of lactose permease of Escherichia coli determined by site-directed chemical labeling and fluorescence spectroscopy. Biochemistry 1995; 34: 8257–13263
  • Sun J., Wu J., Carrasco N., Kaback H. R. Identification of the epitope for monoclonal antibody 481 which uncouples lactose and proton translocation in the lactose permease of Escherichia coli. Biochemistry 1996; 35: 990–998
  • Sun J., Li H., Carrasco N., Kaback H. R. The last two cytoplasmic loops in the lactose permease of Escherichia coli comprise a discontinuous epitope for a monoclonal antibody. Biochemistry 1997; 36: 274–280
  • Popot J. L. Integral membrane protein structure-transmembrane alpha-helices as autonomous folding domains. Current Opinions Structural Biology 1993; 3: 532–540
  • Anfinsen C. B., Scheraga H. A. Experimental and theoretical aspects of protein folding. Advances Protein Chemistry 1975; 29: 205–300
  • Jaenicke R. Protein folding: local structures, domains, subunits, and assemblies. Biochemistry 1991; 30: 3147–3161
  • Wetlaufer D. B., Ristow S. Acquisition of three-dimensional structure of proteins. Annual Review of Biochemistry 1973; 42: 135–158
  • Albert A. D., Litman B. J. Independent structural domains in the membrane protein bovine rhodopsin. Biochemistry 1978; 17: 3893–3900
  • le Coutre J., Narasimhan L. R., Patel C. K. N., Kaback H. R. The lipid bilayer determined helical tilt angle and function in lactose permease of Escherichia coli— an ATR-FTIR study. Proceedings National Academy Science USA 1997; 94: 10167–10171
  • Dunten R. L., Sahin-Toth M., Kaback H. R. Role of the charge pair formed by aspartic acid 237 and lysine 358 in the lactose permease of Escherichia coli. Biochemistry 1993; 32: 3139–3145
  • Bochkareva E., et al. Chaperonin-promoted post-translational membrane insertion of a multispanning membrane protein lactose permease. Journal Biological Chemistry 1996; 271: 22256–22261
  • Consler T. G., Persson B. L., Jung H., Zen K. H., Jung K., Prive G. G., Verner G. E., Kaback H. R. Properties and purification of an active biotinylated lactose permease from Escherichia coli. Proceedings National Academy Science USA 1993; 90: 6934–6938
  • Newman M. J., Foster D. L., Wilson T. H., Kaback H. R. Purification and reconstitution of functional lactose carrier from Escherichia coli. Journal of Biological Chemical 1981; 256: 11804–11808
  • Haugland R. P. Handbook of Fluorescent Probes and Research Chemicals5th edn. Molecular Probes Inc., Eugene, OR 1994

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.