Biomolecular NMR Assignments, volume 12, issue 1, pages 57-62

Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha

Efimov Sergey V 3
Petrova Olga A 4
Rodina Elena V. 2
Klochkov Vladimir V 3
Dontsova Olga A. 2, 4, 5
Publication typeJournal Article
Publication date2017-09-15
Quartile SCImago
Q3
Quartile WOS
Q4
Impact factor0.9
ISSN18742718, 1874270X
Biochemistry
Structural Biology
Abstract
Telomerase is a multisubunit ribonucleoprotein enzyme that is essential for continuous cellular proliferation. A key role of telomerase in cancer and ageing makes it a promising target for the development of cancer therapies and treatments of other age-associated diseases, since telomerase allows unlimited proliferation potential of cells in the majority of cancer types. However, the structure and molecular mechanism of telomerase action are still poorly understood. In budding yeast, telomerase consists of the catalytic subunit, the telomerase reverse transcriptase or Est2 protein, telomerase RNA (TLC1) and two regulatory subunits, Est1 and Est3. Each of the four subunits is essential for in vivo telomerase function. Est3 interacts directly with Est1 and Est2, and stimulates Est2 catalytic activity. However, the exact role of the Est3 protein in telomerase function is still unknown. Determination of the structure, dynamic and functional properties of Est3 can bring new insights into the molecular mechanism of telomerase activity. Here we report nearly complete 1H, 13C and 15N resonance assignments of Est3 from the yeast Hansenula polymorpha. Analysis of the assigned chemical shifts allowed us to identify the protein’s secondary structure and backbone dynamic properties. Structure-based sequence alignment revealed similarities in the structural organization of yeast Est3 and mammalian TPP1 proteins.

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Mariasina S. S. et al. Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha // Biomolecular NMR Assignments. 2017. Vol. 12. No. 1. pp. 57-62.
GOST all authors (up to 50) Copy
Mariasina S. S., Efimov S. V., Petrova O. A., Rodina E. V., Malyavko A. N., Zvereva M. I., Klochkov V. V., Dontsova O. A., Polshakov V. I. Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha // Biomolecular NMR Assignments. 2017. Vol. 12. No. 1. pp. 57-62.
RIS |
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TY - JOUR
DO - 10.1007/s12104-017-9780-5
UR - https://doi.org/10.1007%2Fs12104-017-9780-5
TI - Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha
T2 - Biomolecular NMR Assignments
AU - Mariasina, Sofia S
AU - Petrova, Olga A
AU - Rodina, Elena V.
AU - Malyavko, Alexander N
AU - Zvereva, Maria I.
AU - Dontsova, Olga A.
AU - Polshakov, Vladimir I.
AU - Efimov, Sergey V
AU - Klochkov, Vladimir V
PY - 2017
DA - 2017/09/15 00:00:00
PB - Springer Nature
SP - 57-62
IS - 1
VL - 12
SN - 1874-2718
SN - 1874-270X
ER -
BibTex |
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@article{2017_Mariasina
author = {Sofia S Mariasina and Olga A Petrova and Elena V. Rodina and Alexander N Malyavko and Maria I. Zvereva and Olga A. Dontsova and Vladimir I. Polshakov and Sergey V Efimov and Vladimir V Klochkov},
title = {Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha},
journal = {Biomolecular NMR Assignments},
year = {2017},
volume = {12},
publisher = {Springer Nature},
month = {sep},
url = {https://doi.org/10.1007%2Fs12104-017-9780-5},
number = {1},
pages = {57--62},
doi = {10.1007/s12104-017-9780-5}
}
MLA
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Mariasina, Sofia S., et al. “Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha.” Biomolecular NMR Assignments, vol. 12, no. 1, Sep. 2017, pp. 57-62. https://doi.org/10.1007%2Fs12104-017-9780-5.
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