Nature Structural and Molecular Biology, volume 17, issue 4, pages 513-518
Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA
Mitchell Meghan
1
,
Gillis Andrew
1
,
Futahashi Mizuko
2
,
Fujiwara Haruhiko
2
,
Skordalakes Emmanuel
1
1
Gene expression and Regulation program, The Wistar Institute, Philadelphia, USA
|
2
Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Kashiwa, Japan
|
Publication type: Journal Article
Publication date: 2010-03-28
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 16.8
ISSN: 15459993, 15459985
Molecular Biology
Structural Biology
Abstract
Telomerase is a specialized DNA polymerase that extends the 3′ ends of eukaryotic linear chromosomes, a process required for genomic stability and cell viability. Here we present the crystal structure of the active Tribolium castaneum telomerase catalytic subunit, TERT, bound to an RNA-DNA hairpin designed to resemble the putative RNA-templating region and telomeric DNA. The RNA-DNA hybrid adopts a helical structure, docked in the interior cavity of the TERT ring. Contacts between the RNA template and motifs 2 and B′ position the solvent-accessible RNA bases close to the enzyme active site for nucleotide binding and selectivity. Nucleic acid binding induces rigid TERT conformational changes to form a tight catalytic complex. Overall, TERT–RNA template and TERT–telomeric DNA associations are remarkably similar to those observed for retroviral reverse transcriptases, suggesting common mechanistic aspects of DNA replication between the two families of enzymes.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Mitchell M. et al. Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA // Nature Structural and Molecular Biology. 2010. Vol. 17. No. 4. pp. 513-518.
GOST all authors (up to 50)
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Mitchell M., Gillis A., Futahashi M., Fujiwara H., Skordalakes E. Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA // Nature Structural and Molecular Biology. 2010. Vol. 17. No. 4. pp. 513-518.
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TY - JOUR
DO - 10.1038/nsmb.1777
UR - https://doi.org/10.1038%2Fnsmb.1777
TI - Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA
T2 - Nature Structural and Molecular Biology
AU - Mitchell, Meghan
AU - Gillis, Andrew
AU - Futahashi, Mizuko
AU - Fujiwara, Haruhiko
AU - Skordalakes, Emmanuel
PY - 2010
DA - 2010/03/28 00:00:00
PB - Springer Nature
SP - 513-518
IS - 4
VL - 17
SN - 1545-9993
SN - 1545-9985
ER -
Cite this
BibTex
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@article{2010_Mitchell,
author = {Meghan Mitchell and Andrew Gillis and Mizuko Futahashi and Haruhiko Fujiwara and Emmanuel Skordalakes},
title = {Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA},
journal = {Nature Structural and Molecular Biology},
year = {2010},
volume = {17},
publisher = {Springer Nature},
month = {mar},
url = {https://doi.org/10.1038%2Fnsmb.1777},
number = {4},
pages = {513--518},
doi = {10.1038/nsmb.1777}
}
Cite this
MLA
Copy
Mitchell, Meghan, et al. “Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA.” Nature Structural and Molecular Biology, vol. 17, no. 4, Mar. 2010, pp. 513-518. https://doi.org/10.1038%2Fnsmb.1777.