Biomolecular NMR Assignments

, Volume 12, Issue 1, pp 57–62 | Cite as

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

  • Sofia S. Mariasina
  • Sergey V. Efimov
  • Olga A. Petrova
  • Elena V. Rodina
  • Alexander N. Malyavko
  • Maria I. Zvereva
  • Vladimir V. Klochkov
  • Olga A. Dontsova
  • Vladimir I. Polshakov


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.


Telomerase Protein NMR Resonance assignment Secondary structure 





Telomere elongation protein


Telomerase reverse transcriptase subunit


Telomere replication protein


Hansenula polymorpha Est3 protein


Saccharomyces cerevisiae Est3 protein


Telomerase N-terminal domain


Telomerase RNA


Telomerase reverse transcriptase subunit


Tobacco etch virus nuclear-inclusion-a endopeptidase


Telomere-binding protein, component of the six-membered shelterin complex



The Russian Science Foundation (Grant 14-14-00598) supported the NMR studies. The Russian Foundation for Basic Research (Grant 15-54-74005 EMBL_a) supported protein cloning, expression and purification. The authors are grateful for the opportunity to use the NMR facilities acquired with the support from the Russian Government Program of Competitive Growth of Kazan Federal University, among the world’s leading academic centers.


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Copyright information

© Springer Science+Business Media B.V. 2017

Authors and Affiliations

  • Sofia S. Mariasina
    • 1
    • 2
  • Sergey V. Efimov
    • 3
  • Olga A. Petrova
    • 4
  • Elena V. Rodina
    • 2
  • Alexander N. Malyavko
    • 2
    • 5
  • Maria I. Zvereva
    • 2
  • Vladimir V. Klochkov
    • 3
  • Olga A. Dontsova
    • 2
    • 4
    • 5
  • Vladimir I. Polshakov
    • 1
  1. 1.Center for Magnetic Tomography and Spectroscopy, Faculty of Fundamental MedicineM.V. Lomonosov Moscow State UniversityMoscowRussia
  2. 2.Department of ChemistryM.V. Lomonosov Moscow State UniversityMoscowRussia
  3. 3.NMR Laboratory, Institute of PhysicsKazan Federal UniversityKazanRussia
  4. 4.A.N. Belozersky Institute of Physico-Chemical BiologyM.V. Lomonosov Moscow State UniversityMoscowRussia
  5. 5.Skolkovo Institute of Science and TechnologyMoscowRussia

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