| Форма представления | Статьи в зарубежных журналах и сборниках |
| Год публикации | 2018 |
| Язык | английский |
|
Ефимов Сергей Владимирович, автор
Клочков Владимир Васильевич, автор
Польшаков Владимир Иванович, автор
|
|
Донцова Ольга , автор
|
| Библиографическое описание на языке оригинала |
Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase / O.A. Petrova, A.B. Mantsyzov, E.V. Rodina, S.V. Efimov, C. Hackenberg, J. Hakanpää, V.V. Klochkov, A.A. Lebedev, A.A. Chugunova, A.N. Malyavko, T.S. Zatsepin, A.V. Mishin, M.I. Zvereva, V.S. Lamzin, O.A. Dontsova, V.I. Polshakov // Nucleic Acids Research. – 2018. – V. 46, no. 3. – P. 1525-1540. – DOI 10.1093/nar/gkx1275 |
| Аннотация |
Telomerase function is based on the dynamic interactions of its catalytic subunit (TERT) with nucleic acids––telomerase RNA, telomeric DNA and the DNA/RNA heteroduplex. Here, we present the crystallographic and NMR structures of the N-terminal (TEN) domain of TERT from the thermotolerant yeast Hansenula polymorpha and demonstrate the structural conservation of the core motif in evolutionarily divergent organisms. We identify the TEN residues that are involved in interactions with the telomerase RNA and in the recognition of the 'fork' at the distal end of the DNA product/RNA template heteroduplex. We propose that the TEN domain assists telomerase biological function and is involved in restricting the size of the heteroduplex during telomere repeat synthesis. |
| Ключевые слова |
telomerase, DNA, molecular structure, NMR |
| Название журнала |
Nucleic Acids Research
|
| URL |
https://academic.oup.com/nar/article/46/3/1525/4774275 |
| Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку |
https://repository.kpfu.ru/?p_id=174693 |
Полная запись метаданных  |
| Поле DC |
Значение |
Язык |
| dc.contributor.author |
Ефимов Сергей Владимирович |
ru_RU |
| dc.contributor.author |
Клочков Владимир Васильевич |
ru_RU |
| dc.contributor.author |
Польшаков Владимир Иванович |
ru_RU |
| dc.contributor.author |
Донцова Ольга |
ru_RU |
| dc.date.accessioned |
2018-01-01T00:00:00Z |
ru_RU |
| dc.date.available |
2018-01-01T00:00:00Z |
ru_RU |
| dc.date.issued |
2018 |
ru_RU |
| dc.identifier.citation |
Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase / O.A. Petrova, A.B. Mantsyzov, E.V. Rodina, S.V. Efimov, C. Hackenberg, J. Hakanpää, V.V. Klochkov, A.A. Lebedev, A.A. Chugunova, A.N. Malyavko, T.S. Zatsepin, A.V. Mishin, M.I. Zvereva, V.S. Lamzin, O.A. Dontsova, V.I. Polshakov // Nucleic Acids Research. – 2018. – V. 46, no. 3. – P. 1525-1540. – DOI 10.1093/nar/gkx1275 |
ru_RU |
| dc.identifier.uri |
https://repository.kpfu.ru/?p_id=174693 |
ru_RU |
| dc.description.abstract |
Nucleic Acids Research |
ru_RU |
| dc.description.abstract |
Telomerase function is based on the dynamic interactions of its catalytic subunit (TERT) with nucleic acids––telomerase RNA, telomeric DNA and the DNA/RNA heteroduplex. Here, we present the crystallographic and NMR structures of the N-terminal (TEN) domain of TERT from the thermotolerant yeast Hansenula polymorpha and demonstrate the structural conservation of the core motif in evolutionarily divergent organisms. We identify the TEN residues that are involved in interactions with the telomerase RNA and in the recognition of the 'fork' at the distal end of the DNA product/RNA template heteroduplex. We propose that the TEN domain assists telomerase biological function and is involved in restricting the size of the heteroduplex during telomere repeat synthesis. |
ru_RU |
| dc.language.iso |
ru |
ru_RU |
| dc.subject |
telomerase |
ru_RU |
| dc.subject |
DNA |
ru_RU |
| dc.subject |
molecular structure |
ru_RU |
| dc.subject |
NMR |
ru_RU |
| dc.title |
Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase |
ru_RU |
| dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
|
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