Open Access
Scientific Reports, volume 10, issue 1, publication number 11109
Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase
Shepelev Nikita M
1, 2
,
Mariasina Sofia S
1, 3
,
Efimov Sergey V
4
,
Petrova Olga A
1
,
Rodina Elena V.
1
,
Zvereva Maria I.
1
,
Dontsova Olga A.
1, 2
,
Publication type: Journal Article
Publication date: 2020-07-06
PubMed ID:
32632130
Multidisciplinary
Abstract
Telomerase is a ribonucleoprotein enzyme, which maintains genome integrity in eukaryotes and ensures continuous cellular proliferation. Telomerase holoenzyme from the thermotolerant yeast Hansenula polymorpha, in addition to the catalytic subunit (TERT) and telomerase RNA (TER), contains accessory proteins Est1 and Est3, which are essential for in vivo telomerase function. Here we report the high-resolution structure of Est3 from Hansenula polymorpha (HpEst3) in solution, as well as the characterization of its functional relationships with other components of telomerase. The overall structure of HpEst3 is similar to that of Est3 from Saccharomyces cerevisiae and human TPP1. We have shown that telomerase activity in H. polymorpha relies on both Est3 and Est1 proteins in a functionally symmetrical manner. The absence of either Est3 or Est1 prevents formation of a stable ribonucleoprotein complex, weakens binding of a second protein to TER, and decreases the amount of cellular TERT, presumably due to the destabilization of telomerase RNP. NMR probing has shown no direct in vitro interactions of free Est3 either with the N-terminal domain of TERT or with DNA or RNA fragments mimicking the probable telomerase environment. Our findings corroborate the idea that telomerase possesses the evolutionarily variable functionality within the conservative structural context.
Citations by journals
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eLife
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eLife
1 publication, 25%
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International Journal of Molecular Sciences
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International Journal of Molecular Sciences
1 publication, 25%
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Current Opinion in Structural Biology
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Current Opinion in Structural Biology
1 publication, 25%
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1
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1
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eLife Sciences Publications
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eLife Sciences Publications
1 publication, 25%
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Multidisciplinary Digital Publishing Institute (MDPI)
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Multidisciplinary Digital Publishing Institute (MDPI)
1 publication, 25%
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Elsevier
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Elsevier
1 publication, 25%
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1
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Shepelev N. M. et al. Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase // Scientific Reports. 2020. Vol. 10. No. 1. 11109
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Shepelev N. M., Mariasina S. S., Mantsyzov A. B., Malyavko A. N., Efimov S. V., Petrova O. A., Rodina E. V., Zvereva M. I., Dontsova O. A., Polshakov V. I. Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase // Scientific Reports. 2020. Vol. 10. No. 1. 11109
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TY - JOUR
DO - 10.1038/s41598-020-68107-x
UR - https://doi.org/10.1038%2Fs41598-020-68107-x
TI - Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase
T2 - Scientific Reports
AU - Shepelev, Nikita M
AU - Mariasina, Sofia S
AU - Malyavko, Alexander N
AU - Petrova, Olga A
AU - Rodina, Elena V.
AU - Zvereva, Maria I.
AU - Dontsova, Olga A.
AU - Polshakov, Vladimir I
AU - Mantsyzov, Alexey B
AU - Efimov, Sergey V
PY - 2020
DA - 2020/07/06 00:00:00
PB - Springer Nature
IS - 1
VL - 10
PMID - 32632130
SN - 2045-2322
ER -
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@article{2020_Shepelev,
author = {Nikita M Shepelev and Sofia S Mariasina and Alexander N Malyavko and Olga A Petrova and Elena V. Rodina and Maria I. Zvereva and Olga A. Dontsova and Vladimir I Polshakov and Alexey B Mantsyzov and Sergey V Efimov},
title = {Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase},
journal = {Scientific Reports},
year = {2020},
volume = {10},
publisher = {Springer Nature},
month = {jul},
url = {https://doi.org/10.1038%2Fs41598-020-68107-x},
number = {1},
doi = {10.1038/s41598-020-68107-x}
}