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Structure and Affinity of Complexes between the DNA-Binding Domain of Swi4 and DNAстатья
- Авторы: Afonin D.A., Geras’kina O.V., Loseva T.V., Kirpichnikov M.P., Studitsky V.M., Feofanov A.V.
- Журнал: Biophysics
- Том: 67
- Номер: 5
- Год издания: 2022
- Издательство: Maik Nauka/Interperiodica Publishing
- Местоположение издательства: Russian Federation
- Первая страница: 700
- Последняя страница: 707
- DOI: 10.1134/S0006350922050037
- Аннотация: The work describes the preparation of the recombinant DNA-binding domain of Swi4 protein, which is a component of the SBF transcription factor of the budding yeast Saccharomyces cerevisiae. Circular dichroism spectroscopy data showed that the structure of the domain involves α-helices (29%), β-sheets (22%), β-turns (21%), and disordered structure (28%). We have studied the interaction of the domain with DNA that contains the SBF SCB (Swi4 Cell-cycle Box) binding site. The formation of the complexes is accompanied by a conformational rearrangement in the protein, which affects at least 10 peptide bonds and leads to a 6% increase in the α-helical content and a concomitant decrease in the β-sheet content. Fluorescence spectroscopy revealed that conformational rearrangements and intermolecular interactions do not affect the regions of the Trp68 and Trp112 residues located near the boundaries of the DNA-binding helix-turn-helix motif. It has been found that the dissociation constant of the complex of the DNA-binding domain of the Swi4 protein with DNA is 20 ± 3 nM.
- Добавил в систему: Афонин Дмитрий Алексеевич