Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies.
The mouse int-6 gene was identified in mammary tumors as an integration site for the mouse mammary tumor virus. Its human counterpart encodes a product that interacts with the Tax viral oncoprotein of the human T cell leukaemia virus type 1. This interaction impedes the localisation of over-expressed Int-6 in nuclear bodies containing the promyelocytic leukaemia gene product (PML). In this study, Int-6 is characterised as a 52 kDa protein that is localised within nuclear bodies in primary lymphocytes. Screening of a human B cell cDNA library for proteins that interact with Int-6 led to isolation of four clones coding for the p110 subunit of eIF3, in accordance with previous detection of Int-6 in purified forms of this translation initiation factor. Another clone was interesting with respect to the subcellular localisation of Int-6. It encodes the Ret finger protein (Rfp) which interacts with PML and localises within a subset of PML nuclear bodies. The interaction of Rfp with Int-6 is mediated through a region in Rfp designated 'Rfp domain', distinct from that involved in the interaction with PML. Int-6 and Rfp are co-localised in certain PML nuclear bodies in lymphocytes and transfection studies in HeLa cells strongly suggest that Rfp triggers translocation of Int-6 to nuclear bodies.
Morris-Desbois
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Laboratoire de Biologie Moléculaire et Cellulaire, UMR 5665 CNRS-ENSL, Allée d'Italie, France. pjalinot@ens-lyon.fr
Bochard
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Reynaud
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Jalinot
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D016475:3T3 Cells; D000818:Animals; D019556:COS Cells; D002467:Cell Nucleus / Q000737:chemistry* / Q000235:genetics; D004268:DNA-Binding Proteins; D039621:Eukaryotic Initiation Factor-3; D005455:Fluorescent Antibody Technique; D017353:Gene Deletion; D006367:HeLa Cells; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016296:Mutagenesis / Q000502:physiology; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014162:Transfection; D020798:Two-Hybrid System Techniques; D044767:Ubiquitin-Protein Ligases; D000070584:Tripartite Motif Proteins
D004268:DNA-Binding Proteins; D039621:Eukaryotic Initiation Factor-3; D009687:Nuclear Proteins; D011518:Proto-Oncogene Proteins; D044767:Ubiquitin-Protein Ligases; C064419:TRIM27 protein, human; D000070584:Tripartite Motif Proteins; C489296:Trim27 protein, mouse