Role of Su(Hw) zinc finger 10 and interaction with CP190 and Mod(mdg4) proteins in recruiting the Su(Hw) complex to chromatin sites in Drosophila

PloS One
Larisa MelnikovaA K Golovnin

Abstract

Su(Hw) belongs to the class of proteins that organize chromosome architecture and boundaries/insulators between regulatory domains. This protein contains a cluster of 12 zinc finger domains most of which are responsible for binding to three different modules in the consensus site. Su(Hw) forms a complex with CP190 and Mod(mdg4)-67.2 proteins that binds to well-known Drosophila insulators. To understand how Su(Hw) performs its activities and binds to specific sites in chromatin, we have examined the previously described su(Hw)f mutation that disrupts the 10th zinc finger (ZF10) responsible for Su(Hw) binding to the upstream module. The results have shown that Su(Hw)f loses the ability to interact with CP190 in the absence of DNA. In contrast, complete deletion of ZF10 does not prevent the interaction between Su(Hw)Δ10 and CP190. Having studied insulator complex formation in different mutant backgrounds, we conclude that both association with CP190 and Mod(mdg4)-67.2 partners and proper organization of DNA binding site are essential for the efficient recruitment of the Su(Hw) complex to chromatin insulators.

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Citations

Mar 18, 2020·Scientific Reports·Marina Yu MazinaNadezhda E Vorobyeva
Jan 16, 2021·International Journal of Molecular Sciences·Olga Kyrchanova, Pavel Georgiev
Dec 6, 2018·G3 : Genes - Genomes - Genetics·Steve E Glenn, Pamela K Geyer
Jun 3, 2021·Genes·Samantha C PetersonStacey L Hanlon

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Methods Mentioned

BETA
transgenic
gypsy
two-hybrid
PCR
immunoprecipitation
Transfection
immunoprecipitations
Y2H
Co-immunoprecipitation
for

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