Comparative aspects of basic chromatin proteins in dinoflagellates.
Previous work on histone-like proteins in dinoflagellates is summarized, together with some new data to give an overview of basic proteins in these algae. The first two dinoflagellates studied were both found to contain one major acid-soluble protein that migrated to the same position in acidic-urea gels. When several other genera were studied however, it became apparent that the histone-like proteins from different dinoflagellates were similar but not identical. In view of the great diversity of living dinoflagellates it is speculated that further differences in dinoflagellate basic chromatin proteins will be revealed. Electrophoretic data from the eukaryotic (endosymbiont) nucleus of Peridinium balticum showed the presence of five major components. It is speculated that two of these proteins represent an H1-like doublet and two others correspond to the highly conserved histones H3 and H4. The fifth component is a new histone that may substitute for H2A and H2B in the nucleosome. Because histones and nucleosomes are present in all higher organisms but completely lacking in procaryotes, studies on basic proteins in dinoflagellates will provides insights into the evolution of histones and eucaryotic chromatin organization.
D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D002843:Chromatin / Q000032:analysis* / Q000648:ultrastructure; D004141:Dinoflagellida / Q000032:analysis*; D006657:Histones / Q000032:analysis; D008854:Microscopy, Electron; D009698:Nucleoproteins / Q000032:analysis*; D013045:Species Specificity; D013194:Staining and Labeling
D002843:Chromatin; D006657:Histones; D009698:Nucleoproteins