Nuclear localization of a DNA-binding C-terminal domain from Balbiani ring coded secretory protein

All known Balbiani ring (BR) genes in Chironomus tentans, coding for giant secretory proteins, the sp-I family, end with a short (110 codons) 3'-end exon which is highly conserved in evolution and is structurally unrelated to the sequences characterizing the core of these proteins. We find that the expressed product, the C-terminal domain, shows sequence-specific DNA binding and that it is likely to be absent in one of the sp-I components, sp-Ib, believed to be coded by the BR2.2 gene. Immunohistochemistry shows that material with reactivity towards antibody against the C-terminal domain is present in the nuclei, and specifically enriched in Balbiani ring 1 and 2. Western blotting of extracts from isolated nuclei demonstrates a component with the same antibody reactivity and of an apparent size somewhat larger than that of the domain. The possibility is discussed that the C-terminal part, which is part of the secretion when derived from some of the BR genes, might be cleaved off and function as a feedback signal to control BR gene activity when derived from the BR2.2 gene.