Open Access
Nucleic Acids Research, volume 47, issue 1, pages 391-405
TOE1 acts as a 3′ exonuclease for telomerase RNA and regulates telomere maintenance
Deng Tingting
1, 2
,
Huang Yan
1, 2
,
Weng Kai
3
,
Lin Song
1, 2
,
Li Yujing
1, 2
,
Shi Guang
1, 2
,
Chen Yali
1, 2
,
Huang Junjiu
1, 2
,
Liu Dan
4
,
Ma Wenbin
1, 2
,
Songyang Z.
1, 2, 4
3
Guangzhou Institute of Pediatrics, Guangzhou Women and Children's Medical Centre, Guangzhou 510623, China
|
4
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA
|
Publication type: Journal Article
Publication date: 2018-10-29
Journal:
Nucleic Acids Research
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 14.9
ISSN: 03051048, 13624962
PubMed ID:
30371886
Genetics
Abstract
Abstract In human cells, telomeres are elongated by the telomerase complex that contains the reverse transcriptase hTERT and RNA template TERC/hTR. Poly(A)-specific ribonuclease (PARN) is known to trim hTR precursors by removing poly(A) tails. However, the precise mechanism of hTR 3′ maturation remains largely unknown. Target of Egr1 (TOE1) is an Asp-Glu-Asp-Asp (DEDD) domain containing deadenylase that is mutated in the human disease Pontocerebella Hypoplasia Type 7 (PCH7) and implicated in snRNA and hTR processing. We have previously found TOE1 to localize specifically in Cajal bodies, where telomerase RNP complex assembly takes place. In this study, we showed that TOE1 could interact with hTR and the telomerase complex. TOE1-deficient cells accumulated hTR precursors, including oligoadenylated and 3′-extended forms, which was accompanied by impaired telomerase activity and shortened telomeres. Telomerase activity in TOE1-deficient cells could be rescued by wild-type TOE1 but not the catalytically inactive mutant. Our results suggest that hTR 3′ end processing likely involves multiple exonucleases that work in parallel and/or sequentially, where TOE1 may function non-redundantly as a 3′-to-5′ exonuclease in conjunction with PARN. Our study highlights a mechanistic link between TOE1 mutation, improper hTR processing and telomere dysfunction in diseases such as PCH7.
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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.
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Deng T. et al. TOE1 acts as a 3′ exonuclease for telomerase RNA and regulates telomere maintenance // Nucleic Acids Research. 2018. Vol. 47. No. 1. pp. 391-405.
GOST all authors (up to 50)
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Deng T., Huang Y., Weng K., Lin S., Li Y., Shi G., Chen Y., Huang J., Liu D., Ma W., Songyang Z. TOE1 acts as a 3′ exonuclease for telomerase RNA and regulates telomere maintenance // Nucleic Acids Research. 2018. Vol. 47. No. 1. pp. 391-405.
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TY - JOUR
DO - 10.1093/nar/gky1019
UR - https://doi.org/10.1093%2Fnar%2Fgky1019
TI - TOE1 acts as a 3′ exonuclease for telomerase RNA and regulates telomere maintenance
T2 - Nucleic Acids Research
AU - Deng, Tingting
AU - Huang, Yan
AU - Weng, Kai
AU - Lin, Song
AU - Chen, Yali
AU - Ma, Wenbin
AU - Songyang, Z.
AU - Li, Yujing
AU - Shi, Guang
AU - Huang, Junjiu
AU - Liu, Dan
PY - 2018
DA - 2018/10/29 00:00:00
PB - Oxford University Press
SP - 391-405
IS - 1
VL - 47
PMID - 30371886
SN - 0305-1048
SN - 1362-4962
ER -
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@article{2018_Deng,
author = {Tingting Deng and Yan Huang and Kai Weng and Song Lin and Yali Chen and Wenbin Ma and Z. Songyang and Yujing Li and Guang Shi and Junjiu Huang and Dan Liu},
title = {TOE1 acts as a 3′ exonuclease for telomerase RNA and regulates telomere maintenance},
journal = {Nucleic Acids Research},
year = {2018},
volume = {47},
publisher = {Oxford University Press},
month = {oct},
url = {https://doi.org/10.1093%2Fnar%2Fgky1019},
number = {1},
pages = {391--405},
doi = {10.1093/nar/gky1019}
}
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MLA
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Deng, Tingting, et al. “TOE1 acts as a 3′ exonuclease for telomerase RNA and regulates telomere maintenance.” Nucleic Acids Research, vol. 47, no. 1, Oct. 2018, pp. 391-405. https://doi.org/10.1093%2Fnar%2Fgky1019.