Detection of sugar-binding sites in the fibrillar and the granular components of the nucleolus: an experimental study in cultured mammalian cells.
The intranucleolar distribution of sugar-binding sites (i.e., lectin-like molecules) was analyzed in segregated nucleoli of actinomycin D-treated HeLa cells. The detection of sugar-binding sites was performed by incubation either of permeabilized nuclei in the presence of fluorescein-labeled neoglycoproteins or of ultrathin sections cut through in situ-fixed nuclei in the presence of gold-labeled neoglycoproteins. In the former case, the fluorescent nucleolar components were identified by comparison with the nucleolar components of similarly treated cells observed in electron microscopy. For the first time, this study reveals the presence of sugar-binding sites in both the fibrillar and the granular components of the nucleolus. In view of the data already reported on the biochemical composition of the nucleolus, some of our results led us to conclude that the nucleolar sugar-binding sites are lectin-like proteins. These proteins could be associated with preribosomes since the nucleolus is the site of both synthesis and stockage of ribosomal precursors. Some results from this study, however, show that the possibility of a relationship between some lectins and a structural component cannot be excluded.
D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002466:Cell Nucleolus / Q000032:analysis* / Q000648:ultrastructure; D003609:Dactinomycin / Q000494:pharmacology; D006023:Glycoproteins / Q000032:analysis*; D006367:HeLa Cells / Q000032:analysis* / Q000648:ultrastructure; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis; D008856:Microscopy, Fluorescence; D009363:Neoplasm Proteins / Q000032:analysis
D006023:Glycoproteins; D008565:Membrane Proteins; D009363:Neoplasm Proteins; D003609:Dactinomycin