ISSN:
1617-4623
Keywords:
Key words Chironomus
;
Secretory proteins
;
DNA-binding
;
A.T-rich DNA tracts
;
DNA bending
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract Balbiani ring genes (BRs), the most active loci in the polytene chromosomes of the salivary gland of the midge Chironomus (Diptera), code for secretory giant peptides (the sp-I family). Evidence previously reported indicated that the conserved C-terminal region of proteins of the sp-I family had DNA-binding properties (assayed with sp-Ia), and one such region, derived from BR2.2, which codes for the product sp-Ib, might occur as a stable independent peptide, being transferred to the nucleus where it is detectable in the large BRs (BR1 and BR2), among other structures, by immunostaining. Here, we show that the C-terminal portion of one of the BR gene products, expressed as a glutathione-S-transferase fusion protein shows preferential affinity for A.T-rich sequences and binds with varying affinity to restriction fragments of the A.T-rich BR1 promoter. The binding was inhibited by di-stamycin, suggesting that the interaction involves the minor groove of the DNA. Analysis of the promoter fragments by gel electrophoresis indicated that most appeared to present a conspicuous bend, as deduced from their anomalous electrophoretic mobilities. Furthermore, the affinity of the C-terminal domain for the different promoter fragments appeared to correlate with the degree of bending. Thus, the C-terminal domain might play a role in controlling gene expression by binding to A.T-rich sequences, including those of the BR genes.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02172370
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