Identifying the determinants in the equatorial domain of Buchnera GroEL implicated in binding Potato leafroll virus

Journal of Virology

Volumn 74, Issue 10, 2000, Pages 4541-4548

  Hogenhout, Saskia A ^a   Van Der Wilk, Frank ^a   Verbeek, Martin ^a   Goldbach, Rob W ^a   Van Den Heuvel, Johannes F J M ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DELETION MUTANT; LUTEOVIRUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO ACIDS; ANIMALS; APHIDS; BINDING SITES; BUCHNERA; GENE DELETION; GROEL PROTEIN; LUTEOVIRUS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SOLANUM TUBEROSUM;

EID: 0034003828     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.10.4541-4548.2000     Document Type: Article

References (35)

1. Bogan, A. A., and K. S. Thorn. 1998. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280:1-9.
2. Boisvert, D. C., J. Wang, Z. Otwinowski, A. L. Horwich, and P. Sigler. 1996. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. Nat. Struct. Biol. 3:170-177.
3. Braig, K., Z. Otwinowski, R. Hegde, D. C. Boisvert, A. Joachimiak, A. L. Horwich, and P. Sigler. 1994. The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371:578-586.
4. Brault, V., J. F. J. M. van den Heuvel, M. Verbeek, V. Ziegler-Graff, A. Reutenauer, E. Herrbach, J.-C. Garaud, H. Guilley, K. Richards, and G. Jonard. 1995. Aphid transmission of beet western yellows luteovirus requires the minor capsid read-through protein P74. EMBO J. 14:650-659.
5. Burnett, B. P., A. L. Horwich, and K. B. Low. 1994. A carhoxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12. J. Bacteriol. 176:6980-6985.
6. Creutz, C. E., A. Liou, S. L. Snyder, A. Brownawell, and K. Willison. 1994. Identification of the major chromaffin granule-binding protein, chromobindin A, as the cytosolic chaperonin CCT (chaperonin containing TCP-1 ). J. Biol. Chem. 269:32035-32038.
7. Davis, S. J., S. Ikemizu, M. K. Wild, and P. A. van der Merwe. 1998. CD2 and the nature of protein interactions mediating cell-cell recognition. Immunol. Rev. 163:217-236.
8. Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
9. Ellis, R. J., and S. M. van der Vies. 1991. Molecular chaperones. Annu. Rev. Biochem. 60:321-347.
10. Fenton, W. A., Y. Kashi, K. Furtak, and A. L. Horwich. 1994. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371:614-619.
11. Filichkin, S. A., S. Brumfield, T. P. Filichkin, and M. Young. 1997. In vitro interactions of the aphid endosymbiotic SymL chaperonin with barley yellow dwarf virus. J. Virol. 71:569-577.
12. Gildow, F. E. 1987. Virus-membrane interactions involved in circulative transmission of luteoviruses by aphids. Curr. Top. Vector Res. 4:93-120.
13. Guex, N., and M. C. Peitsch. 1997. SWISS-MODEL and the Swiss-Pdb-Viewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
14. Gupta, R. S. 1995. Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of protein and the origin of eukaryotic cells. Mol. Microbiol. 15:1-11.
15. Gupta, R. S., D. J. Picketts, and S. Ahmad. 1989. A novel ubiquitous protein 'chaperonin' supports the endosymbiotic origin of mitochondrion and plant protoplasts. Biochem. Biophys. Res. Commun. 163:780-787.
16. Hemmingsen, S. M., C. Woolford, S. M. van der Vies, K. Tilly, D. T. Dennis, C. P. Georgopoulos, R. W. Hendrix, and R. J. Ellis. 1988. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333: 330-334.
17. Hogenhout, S. A., F. van der Wilk, M. Verbeek, R. W. Goldbach, and J. F. J. M. van den Heuvel. 1998. Potato leafroll virus binds to the equatorial domain of the aphid endosymbiotic GroEL homolog. J. Virol. 72:358-365.
18. Hogenhout, S. A., M. Verbeek, F. Hans, P. M. Houterman, M. Fortass, F. van der Wilk, H. Huttinga, and J. F. J. M. van den Heuvel. 1996. Molecular bases of the interactions between luteoviruses and aphids. Agronomie 16:167-173.
19. Horowitz, A., E. S. Bochkareva, O. Kovalenko, and A. S. Girshovich. 1993. Mutation Ala2→Ser destabilizes intersubunit interactions in the molecular chaperone GroEL. J. Mol. Biol. 231:58-64.
20. Kim, S., K. R. Willison, and A. L. Horwich. 1994. Cytosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends Biochem. Sci. 19:543-548.
21. Kubota, H., T. Morita, T. Nagata, Y. Takemoto, M. Nozaki, G. Gachelin, and A. Matsushiro. 1991. Nucleotide sequence of mouse Tcp-1a cDNA. Gene 105:269-273.
22. Luo, G.-X., and P. M. Horowitz. 1994. The stability of the molecular chaperonin cnp60 is affected by site-directed replacement of cysteine 518. J. Biol. Chem. 269:32151-32154.
23. Marco, S., J. L. Carrascosa, and J. M. Valpuesta. 1994. Reversible interaction of beta-actin along the channel of the TCP-1 cytoplasmic chaperonin. Biophys. J. 67:364-368.
24. Melki, R., and N. J. Cowan. 1994. Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates. Mol. Cell. Biol. 14:2895-2904.
25. Morin, S., M. Ghanim, M. Zeidan, H. Czosnek, M. Verbeek, and J. F. J. M. van den Heuvel. 1999. A GroEL homologue from endosymbiotic bacteria of the whitefly Bemisia tabaci is implicated in the circulative transmission of tomato yellow leaf curl virus. Virology 256:75-84.
26. Mummert, E., R. Grimm, V. Speth, C. Eckerskorn, E. Schiltz, A. A. Gatenby, and E. Schäfer. 1993. A TCPl-related molecular chaperone from plants refolds phytochrome to its photoreversible form. Nature 363:644-648.
27. Ohtaka, C., H. Nakamura, and H. Ishikawa. 1992. Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants. J. Bacteriol. 174:1869-1874.
28. Singh, J., E. Garber, H. van Vlijmen, M. Karpusas, Y. M. Hsu, Z. Zheng, J. H. Naismith, and D. Thomas. 1998. The role of polar interactions in the molecular recognition of CD40L with its receptor CD40. Protein Sci. 7:1124-1135.
29. Sylvester, E. S. 1980. Circulative and propagative virus transmission by aphids. Annu. Rev. Entomol. 25:257-286.
30. Trent, J. D., E. Nimmesgern, J. S. Wall, F. U. Hartl, and A. L. Horwich. 1991. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 354:490-493.
31. van den Heuvel, J. F. J. M., T. M. Boerma, and D. Peters. 1991. Transmission of potato leafroll virus from plants and artificial diets by Myzus persicae. Phytopathology 81:150-154.
32. van den Heuvel, J. F. J. M., A. Bruyère, S. A. Hogenhout, V. Ziegler-Graff, V. Brault, M. Verbeek, F. van der Wilk, and K. Richards. 1997. The N-terminal region of the luteovirus readthrough domain determines virus binding to Buchnera GroEL and is essential for virus persistence in the aphid. J. Virol. 71:7258-7265.
33. van den Heuvel, J. F. J. M., C. M. de Blank, D. Peters, and J. W. M. van Lent. 1995. Localization of potato leafroll virus in leaves of secondarily-infected potato plants. Eur. J. Plant Pathol. 101:567-571.
34. van den Heuvel, J. F. J. M., M. Verbeek, and F. van der Wilk. 1994. Endosymbiotic bacteria associated with circulative transmission of potato leafroll virus by Myzus persicae. J. Gen. Virol. 75:2559-2565.
35. van der Wilk, F., M. J. Huisman, B. J. C. Cornelissen, H. Huttinga, and R. Goldbach. 1989. Nucleotide sequence and organization of potato leafroll virus genomic RNA. FEBS Lett. 245:51-56.