TRiC-P5, a novel TCP1-related protein, is localized in the cytoplasm and in the nuclear matrix.
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.
Joly
E C
EC
Institut du Cancer de Montréal, Centre de Recherche Louis-Charles Simard, Québec, Canada.
Tremblay
E
E
Tanguay
R M
RM
Wu
Y
Y
Bibor-Hardy
V
V
D056404:Chaperonin Containing TCP-1; D018833:Chaperonins; D003593:Cytoplasm / Q000737:chemistry*; D018076:DNA, Complementary / Q000235:genetics; D015698:Genomic Library; D006801:Humans; D007399:Interphase / Q000502:physiology; D008856:Microscopy, Fluorescence; D018832:Molecular Chaperones / Q000032:analysis*; D009363:Neoplasm Proteins / Q000032:analysis*; D015530:Nuclear Matrix / Q000737:chemistry*; D009687:Nuclear Proteins / Q000032:analysis*; D013347:Subcellular Fractions / Q000737:chemistry; D014407:Tumor Cells, Cultured
C533299:CCT3 protein, human; D018076:DNA, Complementary; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; C533304:TCP1 protein, human; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins