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Joly, EC, Tremblay, E, Tanguay, RM, Wu, Y and Bibor-Hardy, V (1994) TRiC-P5, a novel TCP1-related protein, is localized in the cytoplasm and in the nuclear matrix. J. Cell. Sci. 107 ( Pt 10):2851-9
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.
Chaperonin Containing TCP-1; Chaperonins; Cytoplasm/chemistry; DNA, Complementary/genetics; Genomic Library; Humans; Interphase/physiology; Microscopy, Fluorescence; Molecular Chaperones/analysis; Neoplasm Proteins/analysis; Nuclear Matrix/chemistry; Nuclear Proteins/analysis; Subcellular Fractions/chemistry; Tumor Cells, Cultured
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