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Nuclear localization of a DNA‐binding C‐terminal domain from Balbiani ring coded secretory protein.
Author(s) -
Botella L.,
Grond C.,
Saiga H.,
Edström J. E.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb03274.x
Subject(s) - biology , terminal (telecommunication) , dna , microbiology and biotechnology , dna binding protein , domain (mathematical analysis) , ring (chemistry) , genetics , computational biology , gene , transcription factor , telecommunications , mathematical analysis , chemistry , mathematics , organic chemistry , computer science
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.