spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Joly, E. C.
Right arrow Articles by Bibor-Hardy, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Joly, E. C.
Right arrow Articles by Bibor-Hardy, V.

Journal of Cell Science, Vol 107, Issue 10 2851-2859, Copyright © 1994 by Company of Biologists

JOURNAL ARTICLES

TRiC-P5, a novel TCP1-related protein, is localized in the cytoplasm and in the nuclear matrix

EC Joly, E Tremblay, RM Tanguay, Y Wu and V Bibor-Hardy
Institut du Cancer de Montreal, Centre de Recherche Louis-Charles Simard, Quebec, Canada.

We have recently reported the cloning of a novel protein, TRiC-P5, with significant homology with protein 1 of the t-complex (TCP1). In the present study, the cellular localization of TRiC-P5 in Raji cells has been determined using an antiserum raised against a 18.5 kDa fusion protein. Results from cell fractionation and immunoblot studies indicate that TRiC-P5 is mainly localized in the cytoplasm. In addition, a significant part of TRiC-P5 is also found in the nucleus where it is attached to the nuclear matrix, a complex filament network involved in essential cellular functions such as DNA replication, and RNA transcription and maturation. Immunofluorescence experiments using the anti-TRiC-P5 antibodies confirm these results. We also provide evidence that, in the cytoplasm, TRiC-P5 is part of a large protein complex, most probably the TCP1-ring complex (TRiC), a hetero-oligomeric ring complex that plays a role of molecular chaperone in the folding of actin and tubulin.


This article has been cited by other articles:


Home page
 J. Virol.Home page
S. Hong, G. Choi, S. Park, A.-S. Chung, E. Hunter, and S. S. Rhee
Type D Retrovirus Gag Polyprotein Interacts with the Cytosolic Chaperonin TRiC
J. Virol., March 15, 2001; 75(6): 2526 - 2534.
[Abstract] [Full Text]


© The Company of Biologists Ltd 1994