Springer Nature
Biomolecular NMR Assignments
,  volume 10 ,  issue 1 ,  pages 183-187

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

Publication type: Journal Article
Publication date: 2015-12-31
Springer Nature
scimago Q3
wos Q4
SJR: 0.349
CiteScore: 1.7
Impact factor: 0.6
ISSN: 18742718, 1874270X
Biochemistry
Structural Biology
Abstract
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.
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Polshakov V. I. et al. NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase // Biomolecular NMR Assignments. 2015. Vol. 10. No. 1. pp. 183-187.
GOST all authors (up to 50) Copy
Polshakov V. I., Petrova O. A., Parfenova Y. Yu., Efimov S. V., Klochkov V. V., Zvereva M. I., Dontsova O. A. NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase // Biomolecular NMR Assignments. 2015. Vol. 10. No. 1. pp. 183-187.
RIS |
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RIS Copy
TY - JOUR
DO - 10.1007/s12104-015-9663-6
UR - http://link.springer.com/10.1007/s12104-015-9663-6
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 Nature
SP - 183-187
IS - 1
VL - 10
PMID - 26721464
SN - 1874-2718
SN - 1874-270X
ER -
BibTex |
Cite this
BibTex (up to 50 authors) Copy
@article{2015_Polshakov,
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},
journal = {Biomolecular NMR Assignments},
year = {2015},
volume = {10},
publisher = {Springer Nature},
month = {dec},
url = {http://link.springer.com/10.1007/s12104-015-9663-6},
number = {1},
pages = {183--187},
doi = {10.1007/s12104-015-9663-6}
}
MLA
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MLA Copy
Polshakov, Vladimir I., et al. “NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.” Biomolecular NMR Assignments, vol. 10, no. 1, Dec. 2015, pp. 183-187. http://link.springer.com/10.1007/s12104-015-9663-6.