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PMID: 11432839 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Human telomerase contains two cooperating telomerase RNA molecules.

The EMBO journal ·Vol. 20 ·No. 13 ·2001-07-02 ·Pages 3526-34

Wenz C, Enenkel B, Amacker M, Kelleher C, Damm K, Lingner J

Abstract

Telomerase uses a short stretch of its intrinsic RNA molecule as template for telomere repeat synthesis. Reverse transcription of the RNA template is catalyzed by the telomerase reverse transcriptase (TERT) protein subunit. We demonstrate that human telomerase reconstituted from recombinant TERT and telomerase RNA runs as a dimer on a gel filtration column and that it contains two telomerase RNA molecules. Significantly, a telomerase heterodimer reconstituted from wild-type and mutant telomerase RNA is barely active when compared with the wild-type homodimer. We conclude that the telomerase RNA templates in the active enzyme are interdependent and functionally cooperate with each other. We discuss models that may explain the biological and enzymatic roles of telomerase dimerization.

MeSH Terms
Base Sequence Catalytic Domain Chromatography, Affinity Cloning, Molecular DNA Primers DNA-Binding Proteins Humans Kinetics Models, Molecular Nucleic Acid Conformation Open Reading Frames Protein Conformation RNA/chemistry,metabolism Recombinant Proteins/chemistry,metabolism Telomerase/chemistry,genetics,metabolism Templates, Genetic Transcription, Genetic
Chemicals
DNA Primers DNA-Binding Proteins Recombinant Proteins telomerase RNA RNA TERT protein, human Telomerase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Wenz C
Swiss Institute for Experimental Cancer Research, CH-1066 Epalinges, Switzerland.
Enenkel B
Amacker M
Kelleher C
Damm K
Lingner J
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
2001-07-02
Pages
3526-34
Language
English
Region
England
NLM ID
8208664
PMCID
PMC125520
Subset
IM
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