Open Access
Nature Communications, volume 9, issue 1, publication number 5430
The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN
Tseng Chi Kang
1, 2, 3
,
Wang Hui-Fang
1, 2, 3
,
Schroeder Morgan R
2, 4
,
Baumann Peter
1, 2, 3, 5, 6
1
Howard Hughes Medical Institute, Kansas City, United States
|
2
Stowers Institute for Medical Research, Kansas City, USA
|
3
Institute of Developmental Biology and Neurobiology, Johannes Gutenberg University, Mainz, Germany
|
4
ArcherDX, Boulder, USA
|
5
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, USA
|
6
Institute of Molecular Biology, Mainz, Germany
|
Publication type: Journal Article
Publication date: 2018-12-17
Journal:
Nature Communications
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 16.6
ISSN: 20411723
PubMed ID:
30575725
General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy
Abstract
Human telomerase RNA (hTR) is transcribed as a precursor that is then posttranscriptionally modified and processed. A fraction of the transcripts is oligoadenylated by TRAMP and either processed into the mature hTR or degraded by the exosome. Here, we characterize the processing of 3′ extended forms of varying length by PARN and RRP6. We show that tertiary RNA interactions unique to the longer transcripts favor RNA degradation, whereas H/ACA RNP assembly stimulates productive processing. Interestingly, the H/ACA complex actively promotes processing in addition to protecting the mature 3′ end. Processing occurs in two steps with longer forms first being trimmed by RRP6 and shorter forms then being processed by PARN. These results reveal how RNA structure and RNP assembly affect the kinetics of processing and degradation and ultimately determine the amount of functional telomerase produced in cells. Telomerase RNA (hTR) is transcribed as a 3′-extended precursor. Here the authors examine the processing of hTR precursors of various lengths and show that processing occurs in distinct steps involving different nucleases PARN and RRP6.
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1 publication, 2.86%
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2
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6
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10
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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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Tseng C. K. et al. The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN // Nature Communications. 2018. Vol. 9. No. 1. 5430
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Tseng C. K., Wang H., Schroeder M. R., Baumann P. The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN // Nature Communications. 2018. Vol. 9. No. 1. 5430
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TY - JOUR
DO - 10.1038/s41467-018-07822-6
UR - https://doi.org/10.1038%2Fs41467-018-07822-6
TI - The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN
T2 - Nature Communications
AU - Tseng, Chi Kang
AU - Wang, Hui-Fang
AU - Schroeder, Morgan R
AU - Baumann, Peter
PY - 2018
DA - 2018/12/17 00:00:00
PB - Springer Nature
IS - 1
VL - 9
PMID - 30575725
SN - 2041-1723
ER -
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@article{2018_Tseng,
author = {Chi Kang Tseng and Hui-Fang Wang and Morgan R Schroeder and Peter Baumann},
title = {The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN},
journal = {Nature Communications},
year = {2018},
volume = {9},
publisher = {Springer Nature},
month = {dec},
url = {https://doi.org/10.1038%2Fs41467-018-07822-6},
number = {1},
doi = {10.1038/s41467-018-07822-6}
}