T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol (original) (raw)
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- Published: 16 July 1992
Nature volume 358, pages 249–252 (1992)Cite this article
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Abstract
THE murine t-complex encodes t-complex polypeptide-1 (TCP1)1, which is constitutively expressed in almost all cells, and upregulated during spermatogenesis2,3. Mammalian sequences have >96% identity with each other, and >60% identity with Drosophila melanogaster and yeast orthologues4–9. TCP1 is essential in yeast9, and is postulated to be the cytosolic mammalian equivalent of groEL10,11. We report here that, in the native state, murine and human TCP1 is distributed throughout the cytosol as an 800K–950K hetero-oligomeric particle in association with four to six unidentified proteins and two Hsp70 heat-shock proteins. Negative-stain electron microscopy indicates that the structure is two stacked rings, 12–16 nm in diameter. Therefore, despite similarities with the chaperonin 60 proteins, these data indicate that TCP1 is biochemically and structurally unique. We suggest that TCP1 may represent one of a family of molecules in the eukaryotic cytosol involved in protein folding and regulated in part by their heteromeric associations.
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Authors and Affiliations
- Institute of Cancer Research, Chester Beatty Laboratories, Fulham Road, London, SW3 6JB, UK
Victoria A. Lewis, Gillian M. Hynes, Dong Zheng, Helen Saibil & Keith Willison - Department of Crystallography, Birkbeck College, London, WC1E 7HX, UK
Dong Zheng & Helen Saibil
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- Victoria A. Lewis
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You can also search for this author inPubMed Google Scholar - Helen Saibil
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Lewis, V., Hynes, G., Zheng, D. et al. T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol.Nature 358, 249–252 (1992). https://doi.org/10.1038/358249a0
- Received: 10 March 1992
- Accepted: 22 May 1992
- Published: 16 July 1992
- Issue Date: 16 July 1992
- DOI: https://doi.org/10.1038/358249a0