Enviar artigo por via de e-mail Drosophila protein Z4 has N-terminal ZAD dimerization domain
- Autores: Bonchuk А.N.1, Georgiev P.G.1
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Afiliações:
- Institute of Gene Biology, Russian Academy of Sciences
- Edição: Volume 518, Nº 1 (2024)
- Páginas: 21-25
- Seção: Articles
- URL: https://journals.rcsi.science/2686-7389/article/view/273218
- DOI: https://doi.org/10.31857/S2686738924050049
- ID: 273218
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Resumo
Drosophila transcription factor Z4 (putzig) is one of the key proteins that determines chromatin structure in Drosophila. It is localized at the boundaries of the “bands” of polytene chromosomes, which, according to modern concepts, correlate with chromatin domains. The Z4 protein is a component of a protein complex that also includes the Chromator and BEAF-32 proteins, which require a conserved domain at the N-terminus of Z4 to interact with them. In this study, we showed that this domain is a ZAD (Zinc-finger associated). Using biochemical methods, the ability of this domain to dimerize was confirmed. A dimer model of this domain was obtained using AlphaFold2, the structure of which was confirmed using small-angle X-ray scattering (SAXS). The dimer structure shows a fold typical of ZAD domains.
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Sobre autores
А. Bonchuk
Institute of Gene Biology, Russian Academy of Sciences
Autor responsável pela correspondência
Email: bonchuk_a@genebiology.ru
Rússia, Moscow
P. Georgiev
Institute of Gene Biology, Russian Academy of Sciences
Email: bonchuk_a@genebiology.ru
Academician of the RAS
Rússia, MoscowBibliografia
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