Biomolecular NMR Assignments, том 12, издание 1, номера страниц: 57-62

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

Тип документаJournal Article
Дата публикации2017-09-15
ИздательSpringer Nature
Название журналаBiomolecular NMR Assignments
Квартиль по SCImagoQ4
Квартиль по Web of ScienceQ4
Импакт-фактор 20210.73
ISSN18742718, 1874270X
Biochemistry
Structural Biology
Краткое описание
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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1. Mariasina S.S. и др. Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha // Biomolecular NMR Assignments. 2017. Т. 12. № 1. С. 57–62.
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TY - JOUR

DO - 10.1007/s12104-017-9780-5

UR - http://dx.doi.org/10.1007/s12104-017-9780-5

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 - Efimov, Sergey V.

AU - Petrova, Olga A.

AU - Rodina, Elena V.

AU - Malyavko, Alexander N.

AU - Zvereva, Maria I.

AU - Klochkov, Vladimir V.

AU - Dontsova, Olga A.

AU - Polshakov, Vladimir I.

PY - 2017

DA - 2017/09/15

PB - Springer Science and Business Media LLC

SP - 57-62

IS - 1

VL - 12

SN - 1874-2718

SN - 1874-270X

ER -

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@article{2017,

doi = {10.1007/s12104-017-9780-5},

url = {https://doi.org/10.1007%2Fs12104-017-9780-5},

year = 2017,

month = {sep},

publisher = {Springer Science and Business Media {LLC}},

volume = {12},

number = {1},

pages = {57--62},

author = {Sofia S. Mariasina and Sergey V. Efimov and Olga A. Petrova and Elena V. Rodina and Alexander N. Malyavko and Maria I. Zvereva and Vladimir V. Klochkov and Olga A. Dontsova and Vladimir I. Polshakov},

title = {Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha}

}

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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 12.1 (2017): 57–62. Crossref. Web.