Open Access
Proceedings of the National Academy of Sciences of the United States of America, volume 108, issue 51, pages 20370-20375
Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA
2
Howard Hughes Medical Institute; and
3
Department of Biological Chemistry, University of Michigan Medical School, 1150 West Medical Center Drive, Ann Arbor, MI 48109
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Publication type: Journal Article
Publication date: 2011-06-17
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 11.1
ISSN: 00278424, 10916490
PubMed ID:
21685334
Multidisciplinary
Abstract
The yeast telomerase regulatory protein Est3 is required for telomere maintenance in vivo, and shares intriguing structural and functional similarities with the mammalian telomeric protein TPP1. Here we report our physical and functional characterizations of Est3 homologues from Candida parapsilosis and Lodderomyces elongisporus, which bear unique N- and C-terminal tails in addition to a conserved central OB fold. We show that these Est3 homologues form stable complexes with the TEN domain of telomerase reverse transcriptase. Efficient complex formation requires both the N- and C-terminal tails, as well as conserved OB fold residues of Est3. Other Est3 homologues devoid of the tails failed to interact strongly with the cognate TEN domains. Remarkably, the C. parapsilosis Est3 alone exhibits no appreciable DNA-binding activity, but can be crosslinked to telomeric DNA in the presence of the TEN domain. A conserved basic residue on the putative DNA-binding surface of CpEst3 is required for efficient crosslinking. Mutating the equivalent residue in Candida albicans Est3 caused telomere attrition. We propose that interaction with the TEN domain unmasks a functionally important nucleic acid-binding activity in Est3. Our findings provide insights on the mechanisms and evolution of a widely conserved and functionally critical telomeric/telomerase component.
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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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Yen W. et al. Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA // Proceedings of the National Academy of Sciences of the United States of America. 2011. Vol. 108. No. 51. pp. 20370-20375.
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Yen W., Chico L., Lei M., Lue N. F. Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA // Proceedings of the National Academy of Sciences of the United States of America. 2011. Vol. 108. No. 51. pp. 20370-20375.
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TY - JOUR
DO - 10.1073/pnas.1017855108
UR - https://doi.org/10.1073%2Fpnas.1017855108
TI - Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA
T2 - Proceedings of the National Academy of Sciences of the United States of America
AU - Yen, Wei-Feng
AU - Chico, Lidia
AU - Lei, Ming
AU - Lue, Neal F
PY - 2011
DA - 2011/06/17 00:00:00
PB - Proceedings of the National Academy of Sciences (PNAS)
SP - 20370-20375
IS - 51
VL - 108
PMID - 21685334
SN - 0027-8424
SN - 1091-6490
ER -
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@article{2011_Yen,
author = {Wei-Feng Yen and Lidia Chico and Ming Lei and Neal F Lue},
title = {Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {2011},
volume = {108},
publisher = {Proceedings of the National Academy of Sciences (PNAS)},
month = {jun},
url = {https://doi.org/10.1073%2Fpnas.1017855108},
number = {51},
pages = {20370--20375},
doi = {10.1073/pnas.1017855108}
}
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MLA
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Yen, Wei-Feng, et al. “Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA.” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 51, Jun. 2011, pp. 20370-20375. https://doi.org/10.1073%2Fpnas.1017855108.