Three-dimensional structure of HIV-1 Rev protein filaments

Journal of Structural Biology

Volumn 121, Issue 1, 1998, Pages 41-52

  Watts, Norman R ^a   Misra, Manoj ^a   Wingfield, Paul T ^a   Stahl, Stephen J ^a   Cheng, Naiqian ^a   Trus, Benes L ^a,b   Steven, Alasdair C ^a   Williams, Robert W ^c  

^a NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c UNIFORMED SERVICES UNIVERSITY OF THE HEALTH SCIENCES   (United States)

Author keywords

AIDS; Cryo electron microscopy; Helical filaments; HIV 1; Image reconstruction; Rev

Indexed keywords

REV PROTEIN;

ARTICLE; CRYOELECTRON MICROSCOPY; HUMAN IMMUNODEFICIENCY VIRUS 1; IMAGE RECONSTRUCTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN POLYMERIZATION; THREE DIMENSIONAL IMAGING;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0031927429     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.3964     Document Type: Article

References (54)

1. Adrian M., Dubochet J., Lepault J., McDowall A. W. Cryo-electron microscopy of viruses. Nature. 308:1984;32-36.
2. Antoni B. A., Stein S., Rabson A. B. Regulation of human immunodeficiency virus infection: Implications for pathogenesis. Adv. Virus Res. 43:1994;53-145.
3. Arrigo S., Chen I. S. Y. Rev is necessary for translation but not cytoplasmic accumulation of HIV-1 vif, vpr, and env/vpu 2 RNAs. Genes Dev. 5:1991;808-819.
4. Auer M., Gremlich H.-U., Seifert J.-M., Daly T. J., Parslow T. G., Casari G., Gstach H. Helix-loop-helix motif in HIV-1 Rev. Biochemistry. 33:1994;2988-2996.
5. Battiste J. L., Hongyuan M., Rao N. S., Tan R., Muhandiram D. R., Kay L. E., Frankel A. D., Williamson J. R. α-helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex. Science. 273:1996;1547-1551.
6. Bevec D., Jaksche H., Oft M., Wöhl T., Himmelspach M., Pacher A., Schebesta M., Koettnitz K., Dobrovnik M., Csonga R., Lottspeich F., Hauber J. Inhibition of replication in lymphocytes by mutants of the Rev cofactor eIF-5A. Science. 271:1996;1858-1860.
7. Bogerd H. P., Fridell R. A., Madore S., Cullen B. R. Identification of a novel cellular co-factor for the Rev/Rex class of retroviral proteins. Cell. 82:1995;485-494.
8. Booy F. P., Newcomb W. W., Trus B. L., Brown J. C., Baker T. S., Steven A. C. Liquid-crystalline phage-like packing of encapsidated DNA in Herpes simplex virus. Cell. 64:1991;1007-1015.
9. Cole J. L., Gehman J. D., Shafer J. A., Kuo L. C. Solution oligomerization of the Rev protein of HIV-1: Implications for function. Biochemistry. 32:1993;11769-11775.
10. Conway J. F., Trus B. L., Booy F. P., Newcomb W. W., Brown J. C., Steven A. C. Visualization of three-dimensional density maps reconstructed from cryoelectron micrographs of viral capsids. J. Struct. Biol. 116:1996;200-208.
11. Cullen B. R. Mechanism of action of regulatory proteins encoded by complex retroviruses. Microbiol. Rev. 56:1992;375-394.
12. Daly T. J., Doten R. C., Rennert P., Auer M., Jaksche H., Donner A., Fisk G., Rusche J. R. Biochemical characterization of binding of multiple HIV-1 Rev monomeric proteins to the Rev response element. Biochemistry. 32:1993;10497-10505.
13. Fisher U., Meyer S., Teufel M., Heckel C., Lührman R., Rautmann G. Evidence that HIV-1 Rev directly promotes the nuclear export of unspliced RNA. EMBO J. 13:1994;4105-4112.
14. Fisher U., Huber J., Boelens W. C., Mattaj I. W., Lührman R. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell. 82:1995;475-483.
15. Fritz C. C., Green M. R. HIV Rev uses a conserved cellular protein export pathway for the nucleocytoplasmic transport of viral RNAs. Curr. Biol. 6:1996;848-854.
16. Gerace L. Nuclear export signals and the fast track to the cytoplasm. Cell. 82:1995;341-344.
17. Görlich D., Mattaj I. W. Nucleocytoplasmic transport. Science. 271:1996;1513-1518.
18. Gregory J., Holmes K. Methods of preparing oriented tobacco mosaic virus sols for X-ray diffraction. J. Mol. Biol. 13:1965;796-801.
19. Hainfeld J. F., Safer D., Wall J. S., Simon M., Li B., Powell R. D. Proceedings of the 52nd Annual Meeting of the Micros. 1994;Society of America, San Francisco. p. 132-133.
20. Heaphy S., Finch J. T., Gait M. J., Karn J., Singh M. Human immunodeficiency virus type 1 regulator of virion expression, Rev, forms nucleo-protein filaments after binding to a purine-rich "bubble" located within the rev-response region of viral RNA. Proc. Natl. Acad. Sci. USA. 88:1991;7366-7370.
21. Heck D. V., Trus B. L., Steven A. C. Three-dimensional structure ofBordetellapertussisfimbriae. J. Struct. Biol. 116:1996;264-269.
22. Iwai S., Pritchard C., Mann D. A., Karn J., Gait M. J. Recognition of the high affinity site in rev-response element RNA by the human immunodeficiency virus type-1 rev protein. Nucleic Acids Res. 20:1992;6465-6472.
23. Jain C., Belasco J. G. A structural model for the HIV-1 Rev-RRE complex deduced from altered-specificity rev variants isolated by a rapid genetic strategy. Cell. 87:1996;115-125.
24. Karn J., Dingwall C., Gait M. J., Heaphy S., Skinner M. A. Eckstein F., Lilley D. M. J. Nucleic Acids and Molecular Biology. 1991;194-218 Springer-Verlag, Berlin.
25. Kim N.-H., Herth W., Vuong R., Chanzy H. The cellulose system in the cell wall ofMicrasterias. J. Struct. Biol. 117:1996;195-203.
26. King R. D., Sternberg M. J. Identification and application of the concepts important for accurate and reliable protein secondary structure prediction. Protein Sci. 5:1996;2298-2310.
27. Kingsman S. M., Kingsman A. J. The regulation of human immunodeficiency virus type-1 gene expression. Eur. J. Biochem. 240:1996;491-507.
28. Kjems J., Frankel A. D., Sharp P. A. Specific regulation of mRNA splicinginvitroby a peptide from HIV-1 Rev. Cell. 67:1993;169-178.
29. Kubota S., Furuta R., Maki M., Hatanaka M. Inhibition of human immunodeficiency virus type 1 rev function by a rev mutant which interferes with nuclear/nucleolar localization of rev. J. Virol. 66:1992;2510-2513.
30. Lawrence J., Cochrane A., Johnson C. V., Perkins A., Rosen C. A. The HIV-1 Rev protein: A model system for coupled RNA transport and translation. New Biol. 3:1991;1220-1232.
31. Levy J. A. Pathogenesis of human immunodeficiency virus. Microbiol. Rev. 57:1993;183-289.
32. Malim M. H., Cullen B. R. HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: Implications for HIV-1 latency. Cell. 65:1991;241-248.
33. Misell D. L. Glauert A. M. Practical Methods in Electron Microscopy. 1978;North-Holland, Amsterdam.
34. Nalin C. M., Purcell R. D., Antelman D., Meuller D., Tomchak L., Wegrzynski B., McCarney E., Toome V., Kramer R., Hsu H.-C. Purification and characterization of recombinant Rev protein of human immunodeficiency virus type-1. Proc. Natl. Acad. Sci. USA. 87:1990;7593-7597.
35. Namba K., Pattanayek R., Stubbs G. Visualization of protein-nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2.9 Å resolution by X-ray fiber diffraction. J. Mol. Biol. 208:1989;307-325.
36. Newman R. H. Two-dimensional crystallization of proteins on lipid monolayers. Electron Microsc. Rev. 14:1991;197-203.
37. Rosen C. A., Fenyoe E. M. Virology, an overview. AIDS. 9:1995;S1-S3.
38. Ruiz T., Ranck J.-L., Diaz-Avalos R., Caspar D. L. D., DeRosier D. J. Electron diffraction of helical particles. Ultramicroscopy. 55:1994;383-395.
39. Steven A. C., Stall R., Steinert P. M., Trus B. L. Metuzals J. Electron Microscopy and Alzheimer's Disease. 1986;31-33 San Francisco Press, San Francisco.
40. Stutz F., Neville M., Rosbash M. Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast. Cell. 82:1995;495-506.
41. Szilvay A. M., Brokstad K. A., Bøe S.-O., Haukenes G., Kalland K.-H. Oligomerization of HIV-1 Rev mutants in the cytoplasm and during nuclear import. Virology. 235:1997;73-81.
42. Thomas D., Schultz P., Steven A. C., Wall J. S. Mass analysis of biological macromolecular complexes by STEM. Biol. Cell. 80:1994;181-192.
43. Thomas S., Hauber J., Casari G. Probing the structure of the HIV-1 transactivator protein by functional analysis. Protein Eng. 10:1997;103-107.
44. Torbet J. Using magnetic orientation to study structure and assembly. Trends Biochem. Sci. 12:1987;327-330.
45. Trus B. L., Kocsis E., Conway J. F., Steven A. C. Digital image processing of electron micrographs: The PIC system-III. J. Struct. Biol. 116:1996;61-67.
46. Trus B. L., Steven A. C. Diffraction patterns from stained and unstained helices: Consistency or contradiction. Ultramicroscopy. 15:1984;325-335.
47. 15N resonance assignments and secondary structure analysis of the HU protein fromBacillus stearothermophilususing two- and three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy. Biochemistry. 33:1994;14858-14870.
48. Wall J. S., Hainfeld J. F. Mass mapping with the scanning transmission electron microscope. Annu. Rev. Biophys. Chem. 15:1986;355-376.
49. Wang H., Stubbs G. Structure determination of cucumber green mottle mosaic virus by X-ray fiber diffraction. Significance for the evolution of tobamoviruses. J. Mol. Biol. 239:1994;371-384.
50. Williams R. W. Protein secondary structure analysis using Raman amide I and amide III spectra. Methods Enzymol. 130:1986;311-331.
51. Wilson H. R. Diffraction of X-rays. 1966;Edward Arnold, London.
52. Wingfield P. T., Stahl S. J., Payton M. A., Venkatesan S., Misra M., Steven A. C. HIV-1 Rev expressed in recombinantEscherichia coli: Purification, polymerization, and conformational properties. Biochemistry. 30:1991;7527-7534.
53. Zapp M. L., Hope T. J., Parslow T. G., Green M. R. Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: A dual function for an arginine-rich binding motif. Proc. Natl. Acad. Sci. USA. 88:1991;7734-7738.
54. Zemmel R. W., Kelley A. C., Karn J., Butler P. J. G. Flexible regions of RNA structure facilitate co-operative Rev assembly on the Rev-response element. J. Mol. Biol. 258:1996;763-777.