Biochemical indication for myristoylation-dependent conformational changes in HIV-1 Nef

Biochemistry

Volumn 45, Issue 7, 2006, Pages 2339-2349

  Breuer, Sebastian ^a   Gerlach, Holger ^a   Kolaric, Branko ^a,c   Urbanke, Claus ^b   Opitz, Norbert ^a   Geyer, Matthias ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^b HANNOVER MEDICAL SCHOOL   (Germany)

^c UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; CYTOLOGY; DEGRADATION; DIMERS; FLUORESCENCE; LIPIDS; MONOMERS; OLIGOMERS; PROTEINS; VIRUSES;

AIDS; MULTIPHOTON EXCITATION; MYRISTOYLATION; PROTEOLYSIS; TRAFFICKING PATHWAYS;

BIOCHEMISTRY;

NEF PROTEIN; PROTEIN N MYRISTOYLTRANSFERASE;

ACQUIRED IMMUNE DEFICIENCY SYNDROME; AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CODON USAGE; CONFORMATIONAL TRANSITION; CYTOSOL; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; HUMAN IMMUNODEFICIENCY VIRUS 1; MASS SPECTROMETRY; MOLECULAR RECOGNITION; MYRISTYLATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN LOCALIZATION; SOLUBILITY; ULTRACENTRIFUGATION; VIRUS LOAD; VIRUS REPLICATION; WESTERN BLOTTING;

BASE SEQUENCE; BLOTTING, WESTERN; CHROMATOGRAPHY, GEL; CODON; GENE PRODUCTS, NEF; HIV-1; MOLECULAR SEQUENCE DATA; MYRISTIC ACIDS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; ULTRACENTRIFUGATION;

ESCHERICHIA COLI; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 33144469859     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052052c     Document Type: Article

References (52)

1. Resh, M. D. (1996) Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins, Cell. Signalling 8, 403-412.
2. Greene, W. C., and Peterlin, B. M. (2002) Charting HIV's remarkable voyage through the cell: Basic science as a passport to future therapy, Nat. Med. 8, 673-680.
3. Renkema, G. H., and Saksela, K. (2000) Interactions of HIV-1 NEF with cellular signal transducing proteins, Front. Biosci. 5, D268-D283.
4. Fackler, O. T., and Baur, A. S. (2002) Live and let die: Nef functions beyond HIV replication, Immunity 16, 493-497.
5. Geyer, M., Fackler, O. T., and Peterlin, B. M. (2001) Structure-function relationships in HIV-1 Nef, EMBO Rep. 2, 580-585.
6. Janardhan, A., Swigut, T., Hill, B., Myers, M. P., and Skowronski, J. (2004) HIV-1 Nef binds the DOCK2-ELMO1 complex to activate Rac and inhibit lymphocyte chemotaxis, PLoS Biol. 2, E6.
7. Renkema, G. H., Manninen, A., Mann, D. A., Harris, M., and Saksela, K. (1999) Identification of the Nef-associated kinase as p21-activated kinase 2, Curr. Biol. 9, 1407-1410.
8. Fackler, O. T., Luo, W., Geyer, M., Alberts, A. S., and Peterlin, B. M. (1999) Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions, Mol. Cell 3, 729-739.
9. Witte, V., Laffert, B., Rosorius, O., Lischka, P., Blume, K., Galler, G., Stilper, A., Willbold, D., D'Aloja, P., Sixt, M., Kolanus, J., Ott, M., Kolanus, W., Schuler, G., and Baur, A. S. (2004) HIV-1 Nef mimics an integrin receptor signal that recruits the polycomb group protein Eed to the plasma membrane, Mol. Cell 13, 179-190.
10. Janvier, K., Craig, H., Hitchin, D., Madrid, R., Sol-Foulon, N., Renault, L., Cherfils, J., Cassel, D., Benichou, S., and Guatelli, J. (2003) HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes, J. Biol. Chem. 278, 8725-8732.
11. Geyer, M., Yu, H., Mandic, R., Linnemann, T., Zheng, Y. H., Fackler, O. T., and Peterlin, B. M. (2002) Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery, J. Biol. Chem. 277, 28521-28529.
12. Madrid, R., Janvier, K., Hitchin, D., Day, J., Coleman, S., Noviello, C., Bouchet, J., Benmerah, A., Guatelli, J., and Benichou, S. (2005) Nef-induced alteration of the early/recycling endosomal compartment correlates with enhancement of HIV-1 infectivity, J. Biol. Chem. 280, 5032-5044.
13. Rose, J. J., Janvier, K., Chandrasekhar, S., Sekaly, R. P., Bonifacino, J. S., and Venkatesan, S. (2005) CD4 down-regulation by HIV-1 and simian immunodeficiency virus (SIV) Nef proteins involves both internalization and intracellular retention mechanisms, J. Biol. Chem. 280, 7413-7426.
14. Harris, M. (1995) The role of myristoylation in the interactions between human immunodeficiency virus type I Nef and cellular proteins, Biochem. Soc. Trans. 23, 557-561.
15. Resh, M. D. (1999) Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins, Biochim. Biophys. Acta 1451, 1-16.
16. Geyer, M., and Peterlin, B. M. (2001) Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef, FEBS Lett. 496, 91-95.
17. Niederman, T. M., Hastings, W. R., and Ratner, L. (1993) Myristoylation-enhanced binding of the HIV-1 Nef protein to T cell skeletal matrix, Virology 197, 420-425.
18. Kaminchik, J., Margalit, R., Yaish, S., Drummer, H., Amit, B., Sarver, N., Gorecki, M., and Panet, A. (1994) Cellular distribution of HIV type 1 Nef protein: identification of domains in Nef required for association with membrane and detergent-insoluble cellular matrix, AIDS Res. Hum. Retroviruses 10, 1003-1010.
19. Coates, K., Cooke, S. J., Mann, D. A., and Harris, M. P. G. (1997) Protein kinase C-mediated phosphorylation of HIV-I nef in human cell lines, J. Biol. Chem. 272, 12289-12294.
20. Fackler, O. T., Kienzle, N., Kremmer, E., Boese, A., Schramm, B., Klimkait, T., Kucherer, C., and Mueller-Lantzsch, N. (1997) Association of human immunodeficiency virus Nef protein with actin is myristoylation dependent and influences its subcellular localization, Eur. J. Biochem. 247, 843-851.
21. Grzesiek, S., Bax, A., Hu, J. S., Kaufman, J., Palmer, I., Stahl, S. J., Tjandra, N., and Wingfield, P. T. (1997) Refined solution structure and backbone dynamics of HIV-1 Nef, Protein Sci. 6, 1248-1263.
22. Lee, C. H., Saksela, K., Mirza, U. A., Chait, B. T., and Kuriyan, J. (1996) Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain, Cell 85, 931-942.
23. Arold, S., Franken, P., Strub, M. P., Hoh, F., Benichou, S., Benarous, R., and Dumas C. (1997) The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling, Structure 5, 1361-1372.
24. Geyer, M., Munte, C. E., Schorr, J., Kellner, R., and Kalbitzer, H. R. (1999) Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein, J. Mol. Biol. 289, 123-138.
25. Duronio, R. J., Reed, S. I., and Gordon, J. I. (1992) Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae, Proc. Natl Acad. Sci. U.S.A. 89, 4129-4133.
26. Lebowitz, J., Lewis, M. S., and Schuck, P. (2002) Modern analytical ultracentrifugation in protein science: a tutorial review, Protein Sci. 11, 2067-2079.
27. Schulte, A., Czudnochowski, N., Barboric, M., Schonichen, A., Blazek, D., Peterlin, B. M., and Geyer, M. (2005) Identification of a cyclin T-binding domain in Hexim1 and biochemical analysis of its binding competition with HIV-1 Tat, J. Biol. Chem. 280, 24968-24977.
28. Kane, J. F. (1995) Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli, Curr. Opin. Biotechnol. 6, 494-500.
29. Franco, M., Chardin, P., Chabre, M., and Paris, S. (1996) Myristoylation-facilitated binding of the G protein ARF1GDP to membrane phospholipids is required for its activation by a soluble nucleotide exchange factor, J. Biol. Chem. 271, 1573-1578.
30. Freund, J., Kellner, R., Houthaeve, T., and Kalbitzer, H. R. (1994) Stability and proteolytic domains of Nef protein from human immunodeficiency virus (HIV) type 1, Eur. J. Biochem. 221, 811-819.
31. Opitz, N., Rothwell, P. J., Oeke, B., and Schwille, P. (2003) Single molecule FCS-based oxygen sensor (O-2-FCSensor): a new intrinsically calibrated oxygen sensor utilizing fluorescence correlation spectroscopy (FCS) with single fluorescent molecule detection sensitivity, Sens. Actuators, B 96, 460-467.
32. Gryczynski, I., Malak, H., Lakowicz, J. R., Cheung, H. C., Robinson, J., and Umeda, P. K. (1996) Fluorescence spectral properties of troponin C mutant F22W with one-, two-, and three-photon excitation, Biophys. J. 71, 3448-3453.
33. Farazi, T. A., Waksman, G., and Gordon, J. I. (2001) The biology and enzymology of protein N-myristoylation, J. Biol. Chem. 276, 39501-39504.
34. Arold, S., Hoh, F., Domergue, S., Birck, C., Delsuc, M. A., Jullien, M., and Dumas, C. (2000) Characterization and molecular basis of the oligomeric structure of HIV-1 Nef protein, Protein Sci. 9, 1137-1148.
35. Dennis, C. A., Baron, A., Grossmann, J. G., Mazaleyrat, S., Harris, M., and Jaeger, J. (2005) Co-translational myristoylation alters the quaternary structure of HIV-1 Nef in solution, Proteins 60, 658-669.
36. Diaspro, A. (2002) Confocal and two-photon microscopy, Wiley-Liss, New York.
37. Bacia, K., and Schwille, P. (2003) A dynamic view of cellular processes by in vivo fluorescence auto- and cross-correlation spectroscopy, Methods 29, 74-85.
38. Arold, S. T., and Baur, A. S. (2001) Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein, Trends Biochem. Sci. 26, 356-363.
39. Denk, W., Strickler, J. H., and Webb, W. W. (1990) Two-photon laser scanning fluorescence microscopy, Science 248, 73-76.
40. Zipfel, W. R., Williams, R. M., and Webb, W. W. (2003) Nonlinear magic: multiphoton microscopy in the biosciences, Nat. Biotechnol. 21, 1369-1377.
41. Lakowicz, J. R., Gryczynski, I., and Gryczynski, Z. (1999) High throughput screening with multiphoton excitation, J. Biomol. Screen. 4, 355-362.
42. He, G. S., Markowicz, P. P., Lin, T. C., and Prasad, P. N. (2002) Observation of stimulated emission by direct three-photon excitation, Nature 415, 767-770.
43. Lakowicz, J. R., and Gryczynski, I. (1992) Tryptophan fluorescence intensity and anisotropy decays of human serum albumin resulting from one-photon and two-photon excitation, Biophys. Chem. 45, 1-6.
44. Hudson, B. S. (1999) An ionization/recombination mechanism for complexity of the fluorescence of tryptophan in proteins, Acc. Chem. Res. 32, 297-300.
45. Nishimura, G., and Kinjo, M. (2003) Visible emission of a photoproduct from tryptophan solution induced by multiphoton excitation: An investigation by intensity fluctuation analysis, J. Phys. Chem. B 107, 6012-6017.
46. Geyer, M., Fackler, O. T., and Peterlin, B. M. (2002) Subunit H of the V-ATPase involved in endocytosis shows homology to beta-adaptins, Mol. Biol. Cell 13, 2045-2056.
47. Antonny, B., Beraud-Dufour, S., Chardin, P., and Chabre, M. (1997) N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange, Biochemistry 36, 4675-4684.
48. McLaughlin, S., and Aderem, A. (1995) The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions, Trends Biochem. Sci. 20, 272-276.
49. Ames, J. B., Ishima, R., Tanaka, T., Gordon, J. I., Stryer, L., and Ikura, M. (1997) Molecular mechanics of calcium-myristoyl switches, Nature 389, 198-202.
50. Hantschel, O., Nagar, B., Guettler, S., Kretzschmar, J., Dorey, K., Kuriyan, J., and Superti-Furga, G. (2003) A myristoyl/phosphotyrosine switch regulates c-Abl, Cell 112, 845-857.
51. Matsubara, M., Jing, T., Kawamura, K., Shimojo, N., Titani, K., Hashimoto, K., and Hayashi, N. (2005) Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo, Protein Sci. 14, 494-503.
52. Tang, C., Loeliger, E., Luncsford, P., Kinde, I., Beckett, D., and Summers, M. F. (2004) Entropic switch regulates myristate exposure in the HIV-1 matrix protein, Proc. Natl. Acad. Sci. U.S.A. 101, 517-522.