Biomolecular NMR Assignments, том 10, издание 1, номера страниц: 183-187

NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase

Тип документаJournal Article
Дата публикации2015-12-31
ИздательSpringer Nature
Название журналаBiomolecular NMR Assignments
Квартиль по SCImagoQ4
Квартиль по Web of ScienceQ4
Импакт-фактор 20210.73
ISSN18742718, 1874270X
Structural Biology
Краткое описание
Telomerase is a ribonucleoprotein enzyme that adds telomeric DNA fragments to the ends of chromosomes. This enzyme is the focus of substantial attention, both because its structure and mechanism of action are still poorly studied, and because of its pivotal roles in aging and cellular proliferation. The use of telomerase as a potential target for the design of new anticancer drugs is also of great interest. The catalytic protein subunit of telomerase (TERT) contains an N-terminal domain (TEN) that is essential for activity and processivity. Elucidation of the structure and dynamics of TEN in solution is important for understanding the molecular mechanism of telomerase activity and for the design of new telomerase inhibitors. To approach this problem, in this study we report the 1H, 13C, and 15N chemical shift assignments of TEN from Ogataea polymorpha. Analysis of the assigned chemical shifts allowed us to identify secondary structures and protein regions potentially involved in interaction with other participants of the telomerase catalytic cycle.
Пристатейные ссылки: 25
Цитируется в публикациях: 5
The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids
Akiyama B.M., Parks J.W., Stone M.D.
Q1 Nucleic Acids Research 2015 цитирований: 28
Open Access
Open access
Telomere regulation in pluripotent stem cells
Huang Y., Liang P., Liu D., Huang J., Songyang Z.
Q1 Protein and Cell 2014 цитирований: 43
Open Access
Open access
Specific features of telomerase RNA from Hansenula polymorpha
Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J., Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V., Skryabin K.G.
Q1 BMC Genomics 2013 цитирований: 72
Open Access
Open access
A Motif in the Vertebrate Telomerase N-Terminal Linker of TERT Contributes to RNA Binding and Telomerase Activity and Processivity
Harkisheimer M., Mason M., Shuvaeva E., Skordalakes E.
Q1 Structure 2013 цитирований: 30
Open Access
Open access
Specific features of telomerase RNA from Hansenula polymorpha
Smekalova E.M., Malyavko A.N., Zvereva M.I., Mardanov A.V., Ravin N.V., Skryabin K.G., Westhof E., Dontsova O.A.
Q1 RNA 2013 цитирований: 13
Open Access
Open access
Novel anticancer therapeutics targeting telomerase
Ruden M., Puri N.
Q1 Cancer Treatment Reviews 2013 цитирований: 197
Hansenula Polymorpha TERT: A Telomerase Catalytic Subunit Isolated in Recombinant Form with Limited Reverse Transcriptase Activity
Smekalova E.M., Petrova O.A., Zvereva M.I., Dontsova O.A.
Q3 Acta Naturae 2012 цитирований: 5
Open Access
Open access
Telomerase: Structure, functions, and activity regulation
Zvereva M.I., Shcherbakova D.M., Dontsova O.A.
Q2 Biochemistry (Moscow) 2010 цитирований: 94
Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA
Mitchell M., Gillis A., Futahashi M., Fujiwara H., Skordalakes E.
Q1 Nature Structural and Molecular Biology 2010 цитирований: 157
TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
Shen Y., Delaglio F., Cornilescu G., Bax A.
Q1 Journal of Biomolecular NMR 2009 цитирований: 2107
Open Access
Open access
Structure of the Tribolium castaneum telomerase catalytic subunit TERT
Gillis A.J., Schuller A.P., Skordalakes E.
Q1 Nature 2008 цитирований: 216
Structure of the RNA-Binding Domain of Telomerase: Implications for RNA Recognition and Binding
Rouda S., Skordalakes E.
Q1 Structure 2007 цитирований: 67
Adult-onset pulmonary fibrosis caused by mutations in telomerase
Tsakiri K.D., Cronkhite J.T., Kuan P.J., Xing C., Raghu G., Weissler J.C., Rosenblatt R.L., Shay J.W., Garcia C.K.
Q1 Proceedings of the National Academy of Sciences of the United States of America 2007 цитирований: 638
Open Access
Open access
Telomerase Mutations in Families with Idiopathic Pulmonary Fibrosis
Armanios M.Y., Chen J.J., Cogan J.D., Alder J.K., Ingersoll R.G., Markin C., Lawson W.E., Xie M., Vulto I., Phillips J.A., Lansdorp P.M., Greider C.W., Loyd J.E.
Q1 New England Journal of Medicine 2007 цитирований: 847
Open Access
Open access
Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase
Jacobs S.A., Podell E.R., Cech T.R.
Q1 Nature Structural and Molecular Biology 2006 цитирований: 139


1. Polshakov V.I. и др. NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase // Biomolecular NMR Assignments. 2015. Т. 10. № 1. С. 183–187.


DO - 10.1007/s12104-015-9663-6

UR -

TI - NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase

T2 - Biomolecular NMR Assignments

AU - Polshakov, Vladimir I.

AU - Petrova, Olga A.

AU - Parfenova, Yulia Yu.

AU - Efimov, Sergey V.

AU - Klochkov, Vladimir V.

AU - Zvereva, Maria I.

AU - Dontsova, Olga A.

PY - 2015

DA - 2015/12/31

PB - Springer Science and Business Media LLC

SP - 183-187

IS - 1

VL - 10

SN - 1874-2718

SN - 1874-270X

ER -

BibTex |


doi = {10.1007/s12104-015-9663-6},

url = {},

year = 2015,

month = {dec},

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

volume = {10},

number = {1},

pages = {183--187},

author = {Vladimir I. Polshakov and Olga A. Petrova and Yulia Yu. Parfenova and Sergey V. Efimov and Vladimir V. Klochkov and Maria I. Zvereva and Olga A. Dontsova},

title = {{NMR} assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase}


Polshakov, Vladimir I. et al. “NMR Assignments of the N-Terminal Domain of Ogataea Polymorpha Telomerase Reverse Transcriptase.” Biomolecular NMR Assignments 10.1 (2015): 183–187. Crossref. Web.