Integral membrane protein fragment recombination after transfer from nanolipoprotein particles to bicelles

Biochemistry

Volumn 52, Issue 52, 2013, Pages 9405-9412

  Lai, Ginny ^a   Renthal, Robert ^a,b  

^a UNIVERSITY OF TEXAS AT SAN ANTONIO   (United States)

^b University of Texas Health Science Center   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEINS; BI-LAYER; BICELLES; CELL-FREE; DISULFIDE CROSS-LINKING; INTEGRAL MEMBRANE PROTEINS; MEMBRANE PROTEINS; NANODISCS;

ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; MIXTURES; OLIGOMERS;

BIOLOGICAL MEMBRANES;

APOLIPOPROTEIN; BACTERIORHODOPSIN; DISULFIDE; MEMBRANE PROTEIN; NANOLIPOPROTEIN PARTICLE; NANOPARTICLE; UNCLASSIFIED DRUG;

ARTICLE; BICELLE; CELL FREE SYSTEM; CONTROLLED STUDY; CROSS LINKING; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; LIGHT SCATTERING; LIPID BILAYER; NONHUMAN; OLIGOMERIZATION; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN SYNTHESIS; PROTEIN TRANSPORT;

EID: 84891515627     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401391c     Document Type: Article

References (35)

1. Koval, M. (2006) Pathways and control of connexin oligomerization Trends Cell Biol. 16, 159-166
2. Kumar, J., Schuck, P., and Mayer, M. L. (2011) Structure and assembly mechanism for heteromeric kainate receptors Neuron 71, 319-331
3. Valles, A. S. and Barrantes, F. J. (2012) Chaperoning α7 neuronal nicotinic acetylcholine receptors Biochim. Biophys. Acta 1818, 718-729
4. Hong, H., Blois, T. M., Cao, Z., and Bowie, J. U. (2010) Method to measure strong protein-protein interactions in lipid bilayers using a steric trap Proc. Natl. Acad. Sci. U.S.A. 107, 19802-19807
5. Fleming, K. G. (2002) Standardizing the free energy change of transmembrane helix-helix interactions J. Mol. Biol. 323, 563-571
6. Kriegsmann, J., Brehs, M., Klare, J. P., Engelhard, M., and Fitter, J. (2009) Sensory rhodopsin II/transducer complex formation in detergent and in lipid bilayers studied with FRET Biochim. Biophys. Acta 1788, 522-531
7. Bayburt, T. H. and Sligar, S. G. (2010) Membrane protein assembly into Nanodiscs FEBS Lett. 584, 1721-1727
8. Chromy, B. A., Arroyo, E., Blanchette, C. D., Bench, G., Benner, H., Cappuccio, J. A., Coleman, M. A., Henderson, P. T., Hinz, A. K., Kuhn, E. A., Pesavento, J. B., Segelke, B. W., Sulchek, T. A., Tarasow, T., Walsworth, V. L., and Hoeprich, P. D. (2007) Different apolipoproteins impact nanolipoprotein particle formation J. Am. Chem. Soc. 129, 14348-14354
9. Wientzek, M., Kay, C. M., Oikawa, K., and Ryan, R. O. (1994) Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change J. Biol. Chem. 269, 4605-4612
10. Ritchie, T. K., Grinkova, Y. V., Bayburt, T. H., Denisov, I. G., Zolnerciks, J. K., Atkins, W. M., and Sligar, S. G. (2009) Chapter 11: Reconstitution of membrane proteins in phospholipid bilayer nanodiscs Methods Enzymol. 464, 211-231
11. Nath, A., Atkins, W. M., and Sligar, S. G. (2007) Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins Biochemistry 46, 2059-2069
12. Bayburt, T. H., Grinkova, Y. V., and Sligar, S. G. (2006) Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs Arch. Biochem. Biophys. 450, 215-222
13. Banerjee, S. and Nimigean, C. M. (2011) Non-vesicular transfer of membrane proteins from nanoparticles to lipid bilayers J. Gen. Physiol. 137, 217-223
14. Katzen, F., Fletcher, J. E., Yang, J. P., Kang, D., Peterson, T. C., Cappuccio, J. A., Blanchette, C. D., Sulchek, T., Chromy, B. A., Hoeprich, P. D., Coleman, M. A., and Kudlicki, W. (2008) Insertion of membrane proteins into discoidal membranes using a cell-free protein expression approach J. Proteome Res. 7, 3535-3542
15. Liao, M. J., London, E., and Khorana, H. G. (1983) Regeneration of the native bacteriorhodopsin structure from two chymotryptic fragments J. Biol. Chem. 258, 9949-9955
16. Nannepaga, S. J., Gawalapu, R., Velasquez, D., and Renthal, R. (2004) Estimation of helix-helix association free energy from partial unfolding of bacterioopsin Biochemistry 43, 550-559
17. Huang, K. S., Bayley, H., Liao, M. J., London, E., and Khorana, H. G. (1981) Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments J. Biol. Chem. 256, 3802-3809
18. Marti, T. (1998) Refolding of bacteriorhodopsin from expressed polypeptide fragments J. Biol. Chem. 273, 9312-9322
19. Kahn, T. W. and Engelman, D. M. (1992) Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment Biochemistry 31, 6144-6151
20. Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., and Sligar, S. G. (2004) Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size J. Am. Chem. Soc. 126, 3477-3487
21. Cantor, C. R. and Schimmel, P. R. (1980) Biophysical Chemistry, W. H. Freeman, San Francisco.
22. Kucerka, N., Tristram-Nagle, S., and Nagle, J. F. (2005) Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains J. Membr. Biol. 208, 193-202
23. Renthal, R. and Haas, P. (1996) Effect of transmembrane helix packing on tryptophan and tyrosine environments in detergent-solubilized bacterio-opsin J. Protein Chem. 15, 281-289
24. Sigrist, H., Wenger, R. H., Kislig, E., and Wuthrich, M. (1988) Refolding of bacteriorhodopsin. Protease V8 fragmentation and chromophore reconstitution from proteolytic V8 fragments Eur. J. Biochem. 177, 125-133
25. Struck, D. K., Hoekstra, D., and Pagano, R. E. (1981) Use of resonance energy transfer to monitor membrane fusion Biochemistry 20, 4093-4099
26. Liao, M. J., Huang, K. S., and Khorana, H. G. (1984) Regeneration of native bacteriorhodopsin structure from fragments J. Biol. Chem. 259, 4200-4204
27. Goren, M. A. and Fox, B. G. (2008) Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex Protein Expression Purif. 62, 171-178
28. Klammt, C., Schwarz, D., Fendler, K., Haase, W., Dotsch, V., and Bernhard, F. (2005) Evaluation of detergents for the soluble expression of α-helical and β-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system FEBS J. 272, 6024-6038
29. Blanchette, C. D., Law, R., Benner, W. H., Pesavento, J. B., Cappuccio, J. A., Walsworth, V., Kuhn, E. A., Corzett, M., Chromy, B. A., Segelke, B. W., Coleman, M. A., Bench, G., Hoeprich, P. D., and Sulchek, T. A. (2008) Quantifying size distributions of nanolipoprotein particles with single-particle analysis and molecular dynamic simulations J. Lipid Res. 49, 1420-1430
30. Renthal, R. (2010) Helix insertion into bilayers and the evolution of membrane proteins Cell. Mol. Life Sci. 67, 1077-1088
31. Valluru, N., Silva, F., Dhage, M., Rodriguez, G., Alloor, S. R., and Renthal, R. (2006) Transmembrane helix-helix association: Relative stabilities at low pH Biochemistry 45, 4371-4377
32. Careaga, C. L. and Falke, J. J. (1992) Thermal motions of surface α-helices in the d -galactose chemosensory receptor. Detection by disulfide trapping J. Mol. Biol. 226, 1219-1235
33. Hiller, C., Kuhhorn, J., and Gmeiner, P. (2013) Class A G-protein-coupled receptor (GPCR) dimers and bivalent ligands J. Med. Chem. 56, 6542-6559
34. Mary, S., Fehrentz, J. A., Damian, M., Gaibelet, G., Orcel, H., Verdie, P., Mouillac, B., Martinez, J., Marie, J., and Baneres, J. L. (2013) Heterodimerization with its splice variant blocks the ghrelin receptor 1a in a non-signaling conformation: A study with a purified heterodimer assembled into lipid discs J. Biol. Chem. 288, 24656-24665
35. Koradi, R., Billeter, M., and Wuthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures J. Mol. Graphics 14, 29-32, 51-55