On the oligomeric state of chloroplast chaperonin 10 and chaperonin 20

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1651, Issue 1-2, 2003, Pages 76-84

  Sharkia, Rajach ^a   Bonshtien, Anat L ^a   Mizrahi, Itzhak ^a   Weiss, Celeste ^a   Niv, Adina ^a   Lustig, Ariel ^b   Viitanen, Paul V ^c   Azem, Abdussalam ^a  

^a TEL AVIV UNIVERSITY   (Israel)

^b UNIVERSITY OF BASEL   (Switzerland)

^c DUPONT COMPANY   (United States)

Author keywords

Chaperonin; Chloroplast; Cpn10; Cpn20; Cpn60; GroES

Indexed keywords

CHAPERONIN; OLIGOMER; ARABIDOPSIS PROTEIN; CPN20 PROTEIN, ARABIDOPSIS; CROSS LINKING REAGENT; MALATE DEHYDROGENASE; POLYMER; PROTEIN SUBUNIT;

ARTICLE; CHLOROPLAST; CONCENTRATION RESPONSE; GEL FILTRATION CHROMATOGRAPHY; MOLECULAR WEIGHT; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CROSS LINKING; SPECTRUM; ULTRACENTRIFUGATION; ANIMAL; ARABIDOPSIS; CHEMISTRY; GENETICS; MACROMOLECULE; METABOLISM; PROTEIN FOLDING; SWINE;

BACTERIA (MICROORGANISMS); HOMO;

ANIMALS; ARABIDOPSIS; ARABIDOPSIS PROTEINS; CHAPERONIN 10; CHAPERONINS; CHLOROPLASTS; CROSS-LINKING REAGENTS; GROEL PROTEIN; MACROMOLECULAR SUBSTANCES; MALATE DEHYDROGENASE; POLYMERS; PROTEIN FOLDING; PROTEIN SUBUNITS; SWINE;

EID: 1242341391     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00237-1     Document Type: Article

References (25)

1. Hendrick J.P., Hartl F.U. The role of molecular chaperones in protein folding. FASEB J. 9:1995;1559-1569.
2. Braig K. Chaperonins. Curr. Opin. Struct. Biol. 8:1998;159-165.
3. Sigler P.B., Xu Z., Rye H.S., Burston S.G., Fenton W.A., Horwich A.L. Structure and function in GroEL-mediated protein folding. Ann. Rev. Biochem. 67:1998;581-608.
4. Mayhew M., da Silva A.C., Martin J., Erdjument-Bromage H., Tempst P., Hartl F.U. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature. 379:1996;420-426.
5. Musgrove J.E., Johnson R.A., Ellis R.J. Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits. Eur. J. Biochem. 163:1987;529-534.
6. Hemmingsen S.M., Ellis R.J. Purification and properties of ribulose bisphosphate carboxylase large-subunit binding protein. Plant Physiol. 80:1986;269-276.
7. Dickson R., Weiss C., Howard R.J., Alldrick S.P., Ellis R.J., Lorimer G., Azem A., Viitanen P.V. Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding. J. Biol. Chem. 275:2000;11829-11835.
8. Hill J.E., Hemmingsen S.M. Arabidopsis thaliana type I and II chaperonins. Cell Stress Chaperones. 6:2001;190-200.
9. Hunt J.F., Weaver A.J., Landry S.J., Gierasch L., Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature. 379:1996;37-45.
10. Baneyx F., Bertsch U., Kalbach C.E., van der Vies S.M., Soll J., Gatenby A.A. Spinach chloroplast cpn21 co-chaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotide-dependent binding to plastid chaperonin 60. J. Biol. Chem. 270:1995;10695-10702.
11. Bertsch U., Soll J., Seetharam R., Viitanen P.V. Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants. Proc. Natl. Acad. Sci. USA. 89:1992;8696-8700.
12. Bertsch U., Soll J. Functional analysis of isolated cpn10 domains and conserved amino acid residues in spinach chloroplast co-chaperonin by site directed mutagenesis. Plant Mol. Biol. 29:1995;1039-1055.
13. Koumoto Y., Shimada T., Kondo M., Takao T., Shimonishi Y., Hara-Nishimura I., Nishimura M. Chloroplast Cpn20 forms a tetrameric structure in Arabidopsis thaliana. Plant J. 17:1999;467-477.
14. Hirohashi T., Nishio K., Nakai M. cDNA sequence and overexpression of chloroplast chaperonin 21 from Arabidopsis thaliana. Biochim. Biophys. Acta. 1429:1999;512-515.
15. Koumoto Y., Shimada T., Kondo M., Hara-Nishimura I., Nishimura M. Chloroplasts have a novel Cpn10 in addition to Cpn20 as co-chaperonins in Arabidopsis thaliana. J. Biol. Chem. 276:2001;29688-29694.
16. Levy-Rimler G., Viitanen P., Weiss C., Sharkia R., Greenberg A., Niv A., Lustig A., Delarea Y., Azem A. The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60. Eur. J. Biochem. 268:2001;3465-3472.
17. Azem A., Oppliger W., Lustig A., Jeno P., Feifel B., Schatz G., Horst M. The mitochondrial hsp70 chaperone system. Effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70. J. Biol. Chem. 272:1997;20901-20906.
18. Eisenstein E., Reddy P., Fisher M.T. Overexpression, purification, and properties of GroES from Escherichia coli. Methods Enzymol. 290:1998;119-135.
19. Viitanen P.V., Bacot K., Dickson R., Webb T. Purification of recombinant plant and animal GroES homologs: chloroplast and mitochondrial chaperonin 10. Methods Enzymol. 290:1998;218-230.
20. Harlow E., Lane D. Antibodies, a Laboratory Manual. 1988;Cold Spring Harbor Laboratory, Cold Spring Harbor.
21. Behlke J., Ristau O., Schonfeld H.J. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. Biochemistry. 36:1997;5149-5156.
22. Azem A., Weiss C., Goloubinoff P. Structural analysis of GroE chaperonin complexes using chemical cross-linking. Methods Enzymol. 290:1998;253-268.
23. Azem A. Use of the Cross-Linking by Bifunctional Reagents for the Determination of the Symmetry of Multisubunit Assemblies and its Application to Invertebrate Respiratory Proteins. 1993;Department of Biochemistry, Tel Aviv University.
24. Azem A., Shaked I., Rosenbusch J.P., Daniel E. Cross-linking of porin with glutardialdehyde: a test for the adequacy of premises of cross-linking theory. Biochim. Biophys. Acta. 1243:1995;151-156.
25. Yehudai-Resheff S., Hirsh M., Schuster G. Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts. Mol. Cell. Biol. 21:2001;5408-5416.