KFU. Card publication. Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase

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FEDERAL UNIVERSITY

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STRUCTURE AND FUNCTION OF THE N-TERMINAL DOMAIN OF THE YEAST TELOMERASE REVERSE TRANS&SHY;CRIPTASE

Form of presentation

Articles in international journals and collections

Year of publication

2018

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Authors, employees of KFU

Efimov Sergey Vladimirovich, author

Klochkov Vladimir Vasilevich, author

Polshakov Vladimir Ivanovich, author

Other authors

Doncova Olga , author

Bibliographic description in the original language

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

Annotation

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.

Keywords

telomerase, DNA, molecular structure, NMR

The name of the journal

Nucleic Acids Research

URL

https://academic.oup.com/nar/article/46/3/1525/4774275

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=174693&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Efimov Sergey Vladimirovich	ru_RU
dc.contributor.author	Klochkov Vladimir Vasilevich	ru_RU
dc.contributor.author	Polshakov Vladimir Ivanovich	ru_RU
dc.contributor.author	Doncova Olga	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/eng/?p_id=174693&p_lang=2	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	Articles in international journals and collections	ru_RU