The fate of heterogeneous nuclear ribonucleoprotein complexes during mitosis.
Using immunochemical techniques, we have examined the macromolecular state of association of the major heterogeneous nuclear ribonucleoprotein (hnRNP) core proteins in mitotic HeLa cells. We find that these proteins are not free but are associated with high-molecular-weight RNA in the form of particles that sediment as a broad band between 80 and 200 S. We have termed these complexes MhnRNP for mitotic hnRNP protein-containing particles. Their quantity, composition, sedimentation coefficients, buoyant density, and sensitivity to dissociating conditions suggest that they are closely related to the hnRNP complexes of interphase cells and may represent hnRNP complexes containing unprocessed or partially processed heterogeneous nuclear RNA that have been released into the cytoplasm during mitosis. Exogenously added RNA does not associate with the MhnRNP nor does it compete for the major MhnRNP proteins. The MhnRNP remain distinct from other ribonucleoprotein complexes and do not associate with ribosomes even though these structures are not separated by a nuclear envelope during mitosis.
D004797:Enzyme-Linked Immunosorbent Assay; D006367:HeLa Cells / Q000166:cytology / Q000378:metabolism; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D006801:Humans; D007700:Kinetics; D008938:Mitosis; D008970:Molecular Weight; D012261:Ribonucleoproteins / Q000302:isolation & purification / Q000378:metabolism*; D014316:Tritium
D034441:Heterogeneous-Nuclear Ribonucleoproteins; D012261:Ribonucleoproteins; D014316:Tritium