Immunolocalization of nucleolar proteins after D-galactosamine-induced inhibition of transcription in rat hepatocytes. Maintenance of association of RNA polymerase I with inactivated nucleolar chromatin.

The fate of defined nucleolar constituents during D-galactosamine-induced inhibition of transcription and the accompanying extensive structural changes such as nucleolar segregation, fragmentation and disappearance of the granular components was studied by light and electron microscopic immunolocalization, using antibodies to different nucleolar components. In contrast to other inhibitors such as actinomycin D, we show that preribosomal components as monitored by a ribosomal protein leave the nucleolus, while a large proportion of RNA polymerase I remains associated with the nucleolar chromatin, i.e. probably the pre-rRNA genes, during inactivation of transcription. These small structures containing the RNA polymerase I are characterized by low electron density and resemble the 'fibrillar centers' of normal nucleoli. The results are discussed in relation to current concepts of the functional topology of the nucleolus.