Open Access
Open access
Nature, volume 484, issue 7393, pages 260-264

Telomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes

Tang Wen 1, 2, 3
Kannan Ram 1, 2, 3
Blanchette Marco 2, 4
Baumann Peter 1, 2, 3
1
 
Howard Hughes Medical Institute, Kansas City, USA
2
 
Stowers Institute for Medical Research, Kansas City, USA
3
 
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA
4
 
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, USA
Publication typeJournal Article
Publication date2012-03-25
Journal: Nature
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor64.8
ISSN00280836, 14764687
PubMed ID:  22446625
Multidisciplinary
Abstract
In most eukaryotes, the progressive loss of chromosome-terminal DNA sequences is counteracted by the enzyme telomerase, a reverse transcriptase that uses part of an RNA subunit as template to synthesize telomeric repeats. Many cancer cells express high telomerase activity, and mutations in telomerase subunits are associated with degenerative syndromes including dyskeratosis congenita and aplastic anaemia. The therapeutic value of altering telomerase activity thus provides ample impetus to study the biogenesis and regulation of this enzyme in human cells and model systems. We have previously identified a precursor of the fission yeast telomerase RNA subunit (TER1) and demonstrated that the mature 3′-end is generated by the spliceosome in a single cleavage reaction akin to the first step of splicing. Directly upstream and partly overlapping with the spliceosomal cleavage site is a putative binding site for Sm proteins. Sm and like-Sm (LSm) proteins belong to an ancient family of RNA-binding proteins represented in all three domains of life. Members of this family form ring complexes on specific sets of target RNAs and have critical roles in their biogenesis, function and turnover. Here we demonstrate that the canonical Sm ring and the Lsm2–8 complex sequentially associate with fission yeast TER1. The Sm ring binds to the TER1 precursor, stimulates spliceosomal cleavage and promotes the hypermethylation of the 5′-cap by Tgs1. Sm proteins are then replaced by the Lsm2–8 complex, which promotes the association with the catalytic subunit and protects the mature 3′-end of TER1 from exonucleolytic degradation. Our findings define the sequence of events that occur during telomerase biogenesis and characterize roles for Sm and Lsm complexes as well as for the methylase Tgs1.

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GOST Copy
Tang W. et al. Telomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes // Nature. 2012. Vol. 484. No. 7393. pp. 260-264.
GOST all authors (up to 50) Copy
Tang W., Kannan R., Blanchette M., Baumann P. Telomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes // Nature. 2012. Vol. 484. No. 7393. pp. 260-264.
RIS |
Cite this
RIS Copy
TY - JOUR
DO - 10.1038/nature10924
UR - https://doi.org/10.1038%2Fnature10924
TI - Telomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes
T2 - Nature
AU - Tang, Wen
AU - Kannan, Ram
AU - Blanchette, Marco
AU - Baumann, Peter
PY - 2012
DA - 2012/03/25 00:00:00
PB - Springer Nature
SP - 260-264
IS - 7393
VL - 484
PMID - 22446625
SN - 0028-0836
SN - 1476-4687
ER -
BibTex |
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BibTex Copy
@article{2012_Tang
author = {Wen Tang and Ram Kannan and Marco Blanchette and Peter Baumann},
title = {Telomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes},
journal = {Nature},
year = {2012},
volume = {484},
publisher = {Springer Nature},
month = {mar},
url = {https://doi.org/10.1038%2Fnature10924},
number = {7393},
pages = {260--264},
doi = {10.1038/nature10924}
}
MLA
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MLA Copy
Tang, Wen, et al. “Telomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes.” Nature, vol. 484, no. 7393, Mar. 2012, pp. 260-264. https://doi.org/10.1038%2Fnature10924.
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