Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Dec 15;90(24):11975–11979. doi: 10.1073/pnas.90.24.11975

Eukaryotic cytosolic chaperonin contains t-complex polypeptide 1 and seven related subunits.

H Rommelaere 1, M Van Troys 1, Y Gao 1, R Melki 1, N J Cowan 1, J Vandekerckhove 1, C Ampe 1
PMCID: PMC48108  PMID: 7903455

Abstract

We have characterized the cytosolic chaperonin from both rabbit reticulocyte lysate and bovine testis. The heteromeric complex contains eight subunits. Partial amino acid sequence data reveal that one of these is t-complex polypeptide 1 (TCP-1), while the other seven are TCP-1-related polypeptides, implicating the existence of a multigene family of TCP-1 homologues. We provide evidence that TCP-1 ring complex from bovine testis can facilitate the folding of both actin and tubulin, although, as in the case of chaperonin from reticulocyte lysate, two cofactors are required for the generation of properly folded tubulin. An additional molecule of TCP-1 may associate with the chaperonin depending on the purification procedure used. We propose that a highly conserved region in these polypeptides and in other chaperonins of the cpn60 chaperone family participates in ATP binding.

Full text

PDF
11975

Images in this article

11976Fig. 1
on p.11976
11977Fig. 2
on p.11977
11977Fig. 3
on p.11977

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ahmad S., Gupta R. S. Cloning of a Chinese hamster protein homologous to the mouse t-complex protein TCP-1: structural similarity to the ubiquitous 'chaperonin' family of heat-shock proteins. Biochim Biophys Acta. 1990 Oct 23;1087(2):253–255. doi: 10.1016/0167-4781(90)90214-m. [DOI] [PubMed] [Google Scholar]
  2. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  3. Frydman J., Nimmesgern E., Erdjument-Bromage H., Wall J. S., Tempst P., Hartl F. U. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J. 1992 Dec;11(13):4767–4778. doi: 10.1002/j.1460-2075.1992.tb05582.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Gao Y., Thomas J. O., Chow R. L., Lee G. H., Cowan N. J. A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell. 1992 Jun 12;69(6):1043–1050. doi: 10.1016/0092-8674(92)90622-j. [DOI] [PubMed] [Google Scholar]
  5. Gao Y., Vainberg I. E., Chow R. L., Cowan N. J. Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin. Mol Cell Biol. 1993 Apr;13(4):2478–2485. doi: 10.1128/mcb.13.4.2478. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gatenby A. A. Protein folding and chaperonins. Plant Mol Biol. 1992 Jul;19(4):677–687. doi: 10.1007/BF00026793. [DOI] [PubMed] [Google Scholar]
  7. Gething M. J., Sambrook J. Protein folding in the cell. Nature. 1992 Jan 2;355(6355):33–45. doi: 10.1038/355033a0. [DOI] [PubMed] [Google Scholar]
  8. HIRS C. H. The oxidation of ribonuclease with performic acid. J Biol Chem. 1956 Apr;219(2):611–621. [PubMed] [Google Scholar]
  9. Hemmingsen S. M., Woolford C., van der Vies S. M., Tilly K., Dennis D. T., Georgopoulos C. P., Hendrix R. W., Ellis R. J. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature. 1988 May 26;333(6171):330–334. doi: 10.1038/333330a0. [DOI] [PubMed] [Google Scholar]
  10. Hendrix R. W. Purification and properties of groE, a host protein involved in bacteriophage assembly. J Mol Biol. 1979 Apr 15;129(3):375–392. doi: 10.1016/0022-2836(79)90502-3. [DOI] [PubMed] [Google Scholar]
  11. Herman I. M. Actin isoforms. Curr Opin Cell Biol. 1993 Feb;5(1):48–55. doi: 10.1016/s0955-0674(05)80007-9. [DOI] [PubMed] [Google Scholar]
  12. Hohn T., Hohn B., Engel A., Wurtz M., Smith P. R. Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly. J Mol Biol. 1979 Apr 15;129(3):359–373. doi: 10.1016/0022-2836(79)90501-1. [DOI] [PubMed] [Google Scholar]
  13. Kabsch W., Mannherz H. G., Suck D., Pai E. F., Holmes K. C. Atomic structure of the actin:DNase I complex. Nature. 1990 Sep 6;347(6288):37–44. doi: 10.1038/347037a0. [DOI] [PubMed] [Google Scholar]
  14. Kabsch W., Vandekerckhove J. Structure and function of actin. Annu Rev Biophys Biomol Struct. 1992;21:49–76. doi: 10.1146/annurev.bb.21.060192.000405. [DOI] [PubMed] [Google Scholar]
  15. Kirchhoff C., Willison K. Nucleotide and amino-acid sequence of human testis-derived TCP1. Nucleic Acids Res. 1990 Jul 25;18(14):4247–4247. doi: 10.1093/nar/18.14.4247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
  17. Lewis V. A., Hynes G. M., Zheng D., Saibil H., Willison K. T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Nature. 1992 Jul 16;358(6383):249–252. doi: 10.1038/358249a0. [DOI] [PubMed] [Google Scholar]
  18. Martel R., Cloney L. P., Pelcher L. E., Hemmingsen S. M. Unique composition of plastid chaperonin-60: alpha and beta polypeptide-encoding genes are highly divergent. Gene. 1990 Oct 15;94(2):181–187. doi: 10.1016/0378-1119(90)90385-5. [DOI] [PubMed] [Google Scholar]
  19. Phipps B. M., Hoffmann A., Stetter K. O., Baumeister W. A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria. EMBO J. 1991 Jul;10(7):1711–1722. doi: 10.1002/j.1460-2075.1991.tb07695.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Reading D. S., Hallberg R. L., Myers A. M. Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature. 1989 Feb 16;337(6208):655–659. doi: 10.1038/337655a0. [DOI] [PubMed] [Google Scholar]
  21. Studier F. W., Moffatt B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol. 1986 May 5;189(1):113–130. doi: 10.1016/0022-2836(86)90385-2. [DOI] [PubMed] [Google Scholar]
  22. Studier F. W., Rosenberg A. H., Dunn J. J., Dubendorff J. W. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 1990;185:60–89. doi: 10.1016/0076-6879(90)85008-c. [DOI] [PubMed] [Google Scholar]
  23. Trent J. D., Nimmesgern E., Wall J. S., Hartl F. U., Horwich A. L. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature. 1991 Dec 12;354(6353):490–493. doi: 10.1038/354490a0. [DOI] [PubMed] [Google Scholar]
  24. Willison K. R., Dudley K., Potter J. Molecular cloning and sequence analysis of a haploid expressed gene encoding t complex polypeptide 1. Cell. 1986 Mar 14;44(5):727–738. doi: 10.1016/0092-8674(86)90839-1. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES