Abstract
Su(Hw) belongs to a class of proteins that organize chromosome architecture, determine promoter activity, and participate in the formation of boundaries/insulators between regulatory domains. This protein contains a cluster of 12 zinc fingers of the C2H2 type, some of which are responsible for binding to the consensus site. The Su(Hw) protein forms a complex with the Mod(mdg4)-67.2 and the CP190 proteins, where the last one binds to all known Drosophila insulators. To further study the functioning of Su(Hw)-dependent complexes, we used the previously described su(Hw)E8 mutation, with inactive seventh zinc finger, which produced the mutant protein losing the ability to bind to the consensus site. The present work shows that the Su(Hw)E8 protein continues to directly interact with the CP190 and Mod(mdg4)-67.2 proteins. Through interaction with Mod(mdg4)-67.2, the Su(Hw)E8 protein can be recruited into Su(Hw)-dependent complexes formed on chromatin and enhance their insulator activity. Our results demonstrate that DNA-unbound Su(Hw)-dependent complexes can be recruited to Su(Hw)-binding sites through specific protein-protein interactions that are stabilized by Mod(mdg4)-67.2.
Published Version
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