Open Access
Nucleic Acids Research, volume 43, issue 11, pages 5537-5549
The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids
1
Department of Molecular, Cell, and Developmental Biology, University of California, Santa Cruz, CA 95064, USA Center for Molecular Biology of RNA, University of California, Santa Cruz, CA 95064, USA.
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2
Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA Center for Molecular Biology of RNA, University of California, Santa Cruz, CA 95064, USA
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3
2Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA
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Publication type: Journal Article
Publication date: 2015-05-04
Journal:
Nucleic Acids Research
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 14.9
ISSN: 03051048, 13624962
PubMed ID:
25940626
Genetics
Abstract
Telomerase is an enzyme that adds repetitive DNA sequences to the ends of chromosomes and consists of two main subunits: the telomerase reverse transcriptase (TERT) protein and an associated telomerase RNA (TER). The telomerase essential N-terminal (TEN) domain is a conserved region of TERT proposed to mediate DNA substrate interactions. Here, we have employed single molecule telomerase binding assays to investigate the function of the TEN domain. Our results reveal telomeric DNA substrates bound to telomerase exhibit a dynamic equilibrium between two states: a docked conformation and an alternative conformation. The relative stabilities of the docked and alternative states correlate with the number of basepairs that can be formed between the DNA substrate and the RNA template, with more basepairing favoring the docked state. The docked state is further buttressed by the TEN domain and mutations within the TEN domain substantially alter the DNA substrate structural equilibrium. We propose a model in which the TEN domain stabilizes short RNA–DNA duplexes in the active site of the enzyme, promoting the docked state to augment telomerase processivity.
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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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Akiyama B. M., Parks J. W., Stone M. D. The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids // Nucleic Acids Research. 2015. Vol. 43. No. 11. pp. 5537-5549.
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Akiyama B. M., Parks J. W., Stone M. D. The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids // Nucleic Acids Research. 2015. Vol. 43. No. 11. pp. 5537-5549.
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TY - JOUR
DO - 10.1093/nar/gkv406
UR - https://doi.org/10.1093%2Fnar%2Fgkv406
TI - The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids
T2 - Nucleic Acids Research
AU - Akiyama, B M
AU - Parks, J. W.
AU - Stone, M D
PY - 2015
DA - 2015/05/04 00:00:00
PB - Oxford University Press
SP - 5537-5549
IS - 11
VL - 43
PMID - 25940626
SN - 0305-1048
SN - 1362-4962
ER -
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@article{2015_Akiyama,
author = {B M Akiyama and J. W. Parks and M D Stone},
title = {The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids},
journal = {Nucleic Acids Research},
year = {2015},
volume = {43},
publisher = {Oxford University Press},
month = {may},
url = {https://doi.org/10.1093%2Fnar%2Fgkv406},
number = {11},
pages = {5537--5549},
doi = {10.1093/nar/gkv406}
}
Cite this
MLA
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Akiyama, B. M., et al. “The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids.” Nucleic Acids Research, vol. 43, no. 11, May. 2015, pp. 5537-5549. https://doi.org/10.1093%2Fnar%2Fgkv406.