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Mutual influence of linker histone H1 amino acid sequence and DNA nucleotide sequence on the linker histone H1 position in chromatosomeстатья Тезисы
Информация о цитировании статьи получена из
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 16 января 2019 г.
- Авторы: Горковец Т.К., Армеев Г.А., Шайтан К.В., Шайтан А.К.
- Журнал: FEBS open bio
- Том: 8
- Номер: Supplement S1
- Год издания: 2018
- Издательство: John Wiley & Sons Inc.
- Местоположение издательства: United States
- Первая страница: 346
- Последняя страница: 346
- DOI: 10.1002/2211-5463.12453
- Аннотация: Linker histone H1 is a part of chromatosome and plays role in the transcription and replication regulation. Known and experimentally obtained chromatosome models suggest two conformation of chromatosome with different binding types for linker histone H5 from G. gallus and Н1 from D. melanogaster. Our work was based on the hypothesis that amino acid sequence has impact on the binding type and on the fact that linker DNA geometry changes upon binding with the linker histone. To study mutual influence of amino acid sequence and DNA nucleotide sequence on the chromatosome conformation we used several molecular modeling methods such as atom-atom interaction analysis, DNA deformation energy analysis and homology modeling. Firstly, we analyzed known structures and proposed linker DNA sequences preferable for each conformation based on the DNA deformation energy. Different linker histone variants were classified by binding types based on their amino acid sequences. After classification we built chromatosome models for human linker histones variants using homology modeling. Atom-atom interaction analysis showed that linker histones has contacts not only with DNA, but with base pairs. Number of these contacts may differ depending on linker histone sequence. Homology models with binding type opposite to classified types showed decreasing number of contacts. We also built models with the suggested preferable DNA sequences, and interactions analysis of these models showed increasing number of contacts. Taken together our results support the hypothesis that not only linker histone amino acid sequence determines chromatosome conformation, but linker DNA also plays role. Interesting, that one linker histone may show both binding types depending on the linker DNA sequence. This hypothesis may be tested via spFRET. In our further studies we would like also to extend our approach to all linker histones with known amino acid sequences.
- Добавил в систему: Горковец Татьяна Константиновна