Open Access
Molecular and Cellular Biology, volume 22, issue 4, pages 1253-1265
Functional Multimerization of Human Telomerase Requires an RNA Interaction Domain in the N Terminus of the Catalytic Subunit
1
Anatomy and Cell Biology Department, McGill University, Montréal, Québec, Canada H3A 2B2, and Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis-Jewish General Hospital, Montréal, Québec, Canada H3T 1E2
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Publication type: Journal Article
Publication date: 2002-02-15
Journal:
Molecular and Cellular Biology
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 5.3
ISSN: 02707306, 10985549
PubMed ID:
11809815
Molecular Biology
Cell Biology
Abstract
ABSTRACT Functional human telomerase complexes are minimally composed of the human telomerase RNA (hTR) and a catalytic subunit (human telomerase reverse transcriptase [hTERT]) containing reverse transcriptase (RT)-like motifs. The N terminus of TERT proteins is unique to the telomerase family and has been implicated in catalysis, telomerase RNA binding, and telomerase multimerization, and conserved motifs have been identified by alignment of TERT sequences from multiple organisms. We studied hTERT proteins containing N-terminal deletions or substitutions to identify and characterize hTERT domains mediating telomerase catalytic activity, hTR binding, and hTERT multimerization. Using multiple sequence alignment, we identified two vertebrate-conserved TERT N-terminal regions containing vertebrate-specific residues that were required for human telomerase activity. We identified two RNA interaction domains, RID1 and RID2, the latter containing a vertebrate-specific RNA binding motif. Mutations in RID2 reduced the association of hTR with hTERT by 50 to 70%. Inactive mutants defective in RID2-mediated hTR binding failed to complement an inactive hTERT mutant containing an RT motif substitution to reconstitute activity. Our results suggest that functional hTERT complementation requires intact RID2 and RT domains on the same hTERT molecule and is dependent on hTR and the N terminus.
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Moriarty T. J. et al. Functional Multimerization of Human Telomerase Requires an RNA Interaction Domain in the N Terminus of the Catalytic Subunit // Molecular and Cellular Biology. 2002. Vol. 22. No. 4. pp. 1253-1265.
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Moriarty T. J., Huard S., Dupuis S., Autexier C. Functional Multimerization of Human Telomerase Requires an RNA Interaction Domain in the N Terminus of the Catalytic Subunit // Molecular and Cellular Biology. 2002. Vol. 22. No. 4. pp. 1253-1265.
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TY - JOUR
DO - 10.1128/MCB.22.4.1253-1265.2002
UR - https://doi.org/10.1128%2FMCB.22.4.1253-1265.2002
TI - Functional Multimerization of Human Telomerase Requires an RNA Interaction Domain in the N Terminus of the Catalytic Subunit
T2 - Molecular and Cellular Biology
AU - Moriarty, Tara J
AU - Huard, Sylvain
AU - Dupuis, Sophie
AU - Autexier, Chantal
PY - 2002
DA - 2002/02/15 00:00:00
PB - American Society for Microbiology
SP - 1253-1265
IS - 4
VL - 22
PMID - 11809815
SN - 0270-7306
SN - 1098-5549
ER -
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@article{2002_Moriarty,
author = {Tara J Moriarty and Sylvain Huard and Sophie Dupuis and Chantal Autexier},
title = {Functional Multimerization of Human Telomerase Requires an RNA Interaction Domain in the N Terminus of the Catalytic Subunit},
journal = {Molecular and Cellular Biology},
year = {2002},
volume = {22},
publisher = {American Society for Microbiology},
month = {feb},
url = {https://doi.org/10.1128%2FMCB.22.4.1253-1265.2002},
number = {4},
pages = {1253--1265},
doi = {10.1128/MCB.22.4.1253-1265.2002}
}
Cite this
MLA
Copy
Moriarty, Tara J., et al. “Functional Multimerization of Human Telomerase Requires an RNA Interaction Domain in the N Terminus of the Catalytic Subunit.” Molecular and Cellular Biology, vol. 22, no. 4, Feb. 2002, pp. 1253-1265. https://doi.org/10.1128%2FMCB.22.4.1253-1265.2002.