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The Drosophila ankyrin repeat protein cactus has a predominantly α‐helical secondary structure
Author(s) -
Gay Nicholas J.,
Ntwasa Monde
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80720-f
Subject(s) - ankyrin repeat , ankyrin , circular dichroism , protein secondary structure , biology , protein structure , cytoplasm , genetics , alpha helix , protein family , biochemistry , gene
The cactus protein is the Drosophila homologue of the mammalian I K B family of cytoplasmic anchor proteins. We have expressed in E. coli and purified a cactus fusion protein, CACT‐Bgl. CACT‐Bgl protein contains the six ankyrin repeat sequences which are necessary for specific binding to the Drosophila rel family transcription factor dorsal. We show that the purified CACT‐Bgl protein can bind specifically to dorsal and, using circular dichroism spectroscopy, that the protein adopts a largely α‐helical secondary structure. A further analysis of the ankyrin repeat domains of cactus, using an improved secondary structure prediction program indicates that the N‐terminal of the repeat will form into a loop structure and the C‐terminal section into an interrupted, amphipathic α‐helix. On the basis of these findings we propose that the ankyrin repeats of cactus fold together into helical bundles interconnected by diverged loops.