Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress

Biophysical Journal

Volumn 93, Issue 10, 2007, Pages 3541-3547

  Vos, Werner L ^a   Schor, Marieke ^a   Nazarov, Petr V ^a   Koehorst, Rob B M ^a   Spruijt, Ruud B ^a   Hemminga, Marcus A ^a,b  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b NONE   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; COAT PROTEIN; MEMBRANE PROTEIN; PROTEIN M13; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; MATHEMATICAL COMPUTING; MOLECULAR MODEL; MUTAGENESIS; PHOSPHOLIPID BILAYER; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STRESS;

EID: 36549080549     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.112698     Document Type: Article

References (36)

1. Mitra, K., I. Ubarretxena-Belandia, T. Taguchi, G. Warren, and D. M. Engelman. 2004. Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol. Proc. Natl. Acad. Sci. USA. 101:4083-4088.
2. Yuan, C., R. J. O'Connell, P. L. Feinberg-Zadek, L. J. Johnston, and S. N. Treistman. 2004. Bilayer thickness modulates the conductance of the BK channel in model membranes. Biophys. J. 86:3620-3633.
3. Duong-Ly, K. C., V. Nanda, W. F. DeGrado, and K. P. Howard. 2005. The conformation of the pore region of the M2 proton channel depends on the lipid bilayer environment. Protein Sci. 14:856-861.
4. Cornelius, F. 2001. Modulation of Na,K-ATPase and Na-ATPase activity by phopholipids and cholesterol. I. Steady-state kinetics. Biochemistry. 40:8842-8851.
5. Lee, A. G. 1998. How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta. 1376:381-390.
6. Liu, F., R. N. A. H. Lewis, R. S. Hodges, and R. N. McElhaney. 2002. Effects of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers. Biochemistry. 41:9197-9207.
7. De Planque, M. R. R., E. Goormaghtigh, D. V. Greathouse, R. E. Koeppe, J. A. W. Kruijtzer, R. M. J. Liskamp, B. De Kruijff, and J. A. Killian. 2001. Sensitivity of single membrane-spanning α-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation. Biochemistry. 40:5000-5010.
8. Yeagle, P. L., M. Bennett, V. Lemaître, and A. Watts. 2006. Transmembrane helices of membrane proteins may flex to satisfy hydrophobic mismatch. Biochim. Biophys. Acta. 1768:530-537.
9. Killian, J. A. 1998. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta. 1376:401-416.
10. Kandasamy, S. K., and R. G. Larson. 2006. Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch. Biophys. J. 90:2326-2343.
11. Ireta, J., J. Neugebauer, M. Scheffler, A. Rojo, and M. Galván. 2005. Structural transitions in the polyalanine α-helix under uniaxial strain. J. Am. Chem. Soc. 127:17241-17244.
12. Pelton, J. T. 2001. Secondary considerations. Science. 16:2175-2176.
13. Goormaghtigh, E., J.-M. Ruysschaert, and V. Raussens. 2006. Evaluation of the information content in infrared spectra of protein secondary structure information. Biophys. J. 90:2946-2957.
14. Vos, W. L., R. B. M. Koehorst, R. B. Spruijt, and M. A. Hemminga. 2005. Membrane-bound conformation of M13 major coat protein: A structure validation through FRET-derived constraints. J. Biol. Chem. 280:38522-38527.
15. Nazarov, P. V., R. B. M. Koehorst, W. L. Vos, V. V. Apanasovich, and M. A. Hemminga. 2006. FRET study of membrane proteins: simulation-based fitting for analysis of membrane protein embedment and association. Biophys. J. 91:454-466.
16. Nazarov, P. V., R. B. M. Koehorst, W. L. Vos, V. V. Apanasovich, and M. A. Hemminga. 2007. FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein. Biophys. J. 92:1296-1305.
17. Papavoine, C. H. M., B. E. C. Christiaans, R. H. A. Folmer, R. N. H. Konings, and C. W. Hilbers. 1998. Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues. J. Mol. Biol. 282:401-419.
18. Marassi, F. M. M., and S. J. Opella. 2003. Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints. Protein Sci. 12:403-411.
19. Stopar, D., J. Štrancar, R. B. Spruijt, and M. A. Hemminga. 2006. Motional restrictions of membrane proteins: a site-directed spin labeling study. Biophys. J. 91:3341-3348.
20. Spruijt, R. B., A. B. Meijer, C. J. A. M. Wolfs, and M. A. Hemminga. 2000. Localization and rearrangement modulation of the N-terminal arm of the membrane-bound major coat protein of bacteriophage M13. Biochim. Biophys. Acta. 1509:311-323.
21. Spruijt, R. B., C. J. A. M. Wolfs, and M. A. Hemminga. 1989. Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13. Biochemistry. 28:9158-9165.
22. Hudson, E. N., and G. Weber. 1973. Synthesis and characterization of two fluorescent sulfhydryl reagents. Biochemistry. 12:4154-4161.
23. Edelhoch, H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry. 6:1948-1954.
24. Nazarov, P. V., V. V. Apanasovich, V. M. Lutkovski, M. M. Yatskou, R. B. M. Koehorst, and M. A. Hemminga. 2004. Artificial neural network modification of simulation-based fitting: application to a protein-lipid system. J. Chem. Inf. Comput. Sci. 44:568-574.
25. Ge, M., and J. H. Freed. 1999. Electron-spin resonance study of aggregation of gramicidin in dipalmitoylphosphatidylcholine bilayers and hydrophobic mismatch. Biophys. J. 76:264-280.
26. Mall, S., R. Broadbridge, R. P. Sharma, J. M. East, and A. G. Lee. 2001. Self-association of model transmembrane α-helices is modulated by lipid structure. Biochemistry. 40:12379-12386.
27. Lewis, B. A., and D. M. Engelman. 1983. Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses. J. Mol. Biol. 166:203-210.
28. Fernandes, F., L. M. S. Loura, M. Prieto, R. B. M. Koehorst, R. B. Spruijt, and M. A. Hemminga. 2003. Dependence of M13 major coat protein oligomerization and the lateral segregation on bilayer composition. Biophys. J. 85:2430-2441.
29. Koehorst, R. B. M., R. B. Spruijt, F. J. Vergeldt, and M. A. Hemminga. 2004. Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy. Biophys. J. 87:1445-1455.
30. Ireta, J., J. Neugebauer, M. Scheffler, A. Rojo, and M. Galváni. 2003. Density functional theory study of the cooperativity of hydrogen bonds in finite and infinite α-helix. J. Phys. Chem. B. 107:1432-1437.
31. Creighton, T. E. 1983. Proteins. Freeman, New York.
32. Caballero-Herrera, A., K. Nordstrand, K. D. Berndt, and L. Nilsson. 2005. Effect of urea on peptide conformation in water: molecular dynamics and experimental characterization. Biophys. J. 89:842-857.
33. Choi, G., J. Landin, J. F. Galan, R. R. Birge, A. D. Albert, and P. L. Yeagle. 2002. Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin. Biochemistry. 41:7318-7324.
34. Zbilut, J. P., A. Colosimo, F. Conti, M. Colafranceschi, C. Manetti, M. Valerio, C. L. Webber, Jr., and A. Giuliani. 2003. Protein aggregation/folding: the role of deterministic singularities of sequence hydrophobicity as determined by nonlinear signal analysis of acylphosphatase and Aβ(1-40). Biophys. J. 85:3544-3557.
35. Stopar, D., R. B. Spruijt, and M. A. Hemminga. 2006. Anchoring mechanisms of membrane-associated M13 major coat protein. Chem. Phys. Lipids. 141:83-93.
36. Mouritsen, O. G., and M. Bloom. 1984. Mattress model of lipid-protein interactions in membranes. Biophys. J. 1984:141-153.