Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo

Archives of Virology

Volumn 143, Issue 11, 1998, Pages 2203-2214

  Hwang, D J ^a,b   Tumer, N E ^a   Wilson, T M A ^a,c  

^a RUTGERS UNIVERSITY   (United States)

^b National Institute of Animal Science   (South Korea)

^c SCOTTISH CROP RESEARCH INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHIMERIC RNA; MUTATION; PROTEIN FOLDING; RIBONUCLEOCAPSID; TOBACCO MOSAIC VIRUS; VIRUS COAT PROTEIN;

BACTERIAL PROTEINS; CAPSID; CAPSID PROTEINS; CHAPERONINS; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; PROTEIN FOLDING; TOBACCO MOSAIC VIRUS; VIRAL PROTEINS; VIRUS ASSEMBLY;

ANIMALIA; ESCHERICHIA COLI; NICOTIANA TABACUM; PROKARYOTA; TOBACCO MOSAIC VIRUS;

EID: 14444281746     PISSN: 03048608     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007050050452     Document Type: Article

References (41)

1. Agranovsky AA, Boyko VP, Karasev AV, Koonin EV, Dolja VV (1991) Putative 65kDa protein of beet yellows closterovirus is a homologue of HSP70 heat shock proteins. J Mol Biol 217: 603-610
2. Agranovsky AA, Folimonova S Yu, Folimonov AS, Denisenko ON, Zinovkin RA (1997) The beet yellows closterovirus p65 homologue of HSP70 chaperones has ATPase activity associated with its conserved N-terrninal domain but does not interact with unfolded protein chains. J Gen Virol 78: 535-542
3. Badcoe IG, Smith CJ, Wood S, Halsall DJ, Holbrook JJ, Lund P, Clark AR (1991) Binding of a chaperonin to the folding intermediates of lactate-dehydrogenase. Biochemistry 30: 9 195-9 200
4. Buchner J, Schmidt M, Fuchs M, Jaenicke R, Rudolph R, Schmid FX, Kiefhaber T (1991) GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 30: 1 586-1 591
5. Butler PJG, Klug A (1971) Assembly of the particle of tobacco mosaic virus from RNA and disks of protein. Nature New Biol 229: 47-50
6. Caspar DLD, Namba K (1990) Switching in the sell-assembly of tobacco mosaic virus. Adv Biophys 26: 157-185
7. Dore I, Weiss E, Altshuh D, Van Regenmortel MHV (1988) Visualization by electron microscopy of the location of tobacco mosaic virus epitopes reacting with monoclonal antibodies in enzyme immunoassay. Virology 162: 279-289
8. Ellis RJ, Van der Vies SM (1991) Molecular chaperones. Ann Rev Biochem 60: 321-347
9. Escher A, Szalay AA (1993) GroE-mediated folding of bacterial luciferase in vivo. Mol Gen Genet 238: 65-73
10. Fayet O, Louarn JM, Georgopoulos C (1986) Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groES genes. Mol Gen Genet 202: 435-445
11. Fayet O, Ziegelhoffer T, Georgopoulos C (1989) The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J Bacteriol 171: 1 379-1 385
12. Gallie DR, Sleat DE, Watts JW, Turner PC, Wilson TMA (1987) The 5′ leader sequence of tobacco mosaic virus RNA enhances the expression of foreign gene transcripts in vitro and in vivo. Nucleic Acids Res 15: 3 257-3 273
13. Gething MJ, Sambrook J (1992) Protein folding in the cell. Nature 355: 33-45
14. Goloubinoff P, Gatenby AA, Lorimer GH (1989) GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 337: 44-47
15. Gordon CL, Sather SK, Casjens S, King J (1994) Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins. J Biol Chem 269: 27 941-27 951
16. Harlow E, Lane D (1988) Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, New York
17. Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-580
18. Hartl FU, Martin J, Neupert W (1992) Protein folding in the cell: role of molecular chaperones Hsp70 and Hsp60. Ann Rev Biophys Biol Struct 21: 293-322
19. Haynes JR, Cunningham J, Von Seefried A, Lennick M, Garvin RT, Shen S-H (1986) Development of a genetically-engineered, candidate polio vaccine employing the self-assembling properties of the tobacco mosaic virus coat protein. Bio/Technology 4: 637-641
20. Hwang D-J, Roberts IM, Wilson TMA (1994) Expression of tobacco mosaic virus coat protein and assembly of pseudovirus particles in Escherichia coli. Proc Natl Acad Sci USA 91: 9 067-9 071
21. Kubo T, Mizobata T, Kawala Y (1993) Refolding of yeast enolase in the presence of the chaperonin GroE. J Biol Chem 268: 19 346-19 351
22. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
23. Laminet AA, Ziegelhoffer T, Georgopoulos C, Pluckthun A (1990) The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor. EMBO J 9: 2 315-2 319
24. Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci USA 88: 2 874-2 878
25. Martin J, Langer T, Boteva R, Schramel A, Horwich AL, Hartl FU (1991) Chaperonin-mediated protein folding at the surface of GroEL through a "molten-globule"-like intermediate. Nature 352: 36-42
26. Martin J, Mayhew M, Langer T, Hartl FU (1993) The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 366: 228-233
27. Mendoza JA, Rogers E, Lorimer GH, Horowitz PM (1991) Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanase. J Biol Chem 266: 13 044-13 049
28. Pappu HR, Karasev AV, Anderson EV, Pappu SS, Hilf ME, Febres VJ, Eckloff RMG, McCaffery M, Boyko V, Gowda S, Dolja VV, Koonin EV, Gumpf DJ, Cline KC, Garnsey SM, Dawson WO, Lee RF, Niblett CL (1994) Nucleotide sequence and organization of eight 3′ open reading frames of the citrus tristeza closterovirus genome. Virology 199: 35-46
29. Sambrook J, Fritsch EF, Maniatis T (1987) Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, New York
30. Shire SJ, McKay P, Leung DW, Cachianes GJ, Jackson E, Wood WI, Raghavendra K, Khairallah L, Schuster T (1990) Preparation and properties of recombinant DNA-derived tobacco mosaic virus coat protein. Biochemistry 29: 5 119-5 126
31. 32. Genes Dev 4: 2 202-2 209
32. Studier FW, Rosenberg AH, Dunn JJ, Dubendorff JW (1990) Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol 185: 60-89
33. Sunshine M, Feiss M, Stuart J, Yochem J (1977) A new host gene (groPC) necessary for lambda DNA replication. Mol Gen Genet 151: 27-34
34. Van der Vies SM, Gatenby AA, Georgopoulos C (1994) Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding. Nature 368: 654-656
35. Van Regenmortel MHV, Buckard J (1980) Detection of a wide spectrum of tobacco mosaic virus strains by indirect enzyme-linked immunosorbent assays (ELISA). Virology 106: 327-334
36. Viitanen PV, Donaldson GK, Lorimer GH, Lubben TH, Gatenby AA (1991) Complex interactions between the chaperonin-60 molecular chaperone and dihydrofolate reductase. Biochemistry 30: 9 716-9 723
37. 7 chaperonin complex. Nature 388: 741-750
38. Yochem J, Uchida H, Sunshine M, Saito H, Georgopoulos CP, Feiss M (1978) Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication. Mol Gen Genet 164: 9-14
39. Zahn R, Pluckthun A (1992) GroE prevents the accumulation of early folding intermediates of pre-ß-lactamase without changing the folding pathway. Biochemistry 31: 3 249-3 255
40. Zeilstra-Ryalls J, Fayet O, Georgopoulos C (1991) The universally conserved GroE (Hsp60) chaperonins. Ann Rev Microbiol 45: 301-325
41. Zimmern D, Wilson TMA (1976) Location of the origin for viral reassembly on tobacco mosaic virus RNA and its relation to stable fragment. FEBS Lett 71: 294-298