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RNA Binding Domain of Telomerase Reverse Transcriptase

Telomerase is a ribonucleoprotein reverse transcriptase that extends the ends of chromosomes. The two telomerase subunits essential for catalysis in vitro are the telomerase reverse transcriptase (TERT) and the telomerase RNA. Using truncations and site-specific mutations, we identified sequence ele...

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Egile Nagusiak:	Lai, Cary K., Mitchell, James R., Collins, Kathleen
Formatua:	Artikulua
Hizkuntza:	en
Argitaratua:	American Society for Microbiology 2001
Gaiak:	DNA Dynamics and Chromosome Structure
Sarrera elektronikoa:	https://ncbi.nlm.nih.gov/pmc/articles/PMC99554/ https://ncbi.nlm.nih.gov/pubmed/11158287 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/MCB.21.4.990-1000.2001
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id	pubmed-99554
record_format	dspace
spelling	pubmed-995542002-09-13 RNA Binding Domain of Telomerase Reverse Transcriptase Lai, Cary K. Mitchell, James R. Collins, Kathleen Mol Cell Biol DNA Dynamics and Chromosome Structure Telomerase is a ribonucleoprotein reverse transcriptase that extends the ends of chromosomes. The two telomerase subunits essential for catalysis in vitro are the telomerase reverse transcriptase (TERT) and the telomerase RNA. Using truncations and site-specific mutations, we identified sequence elements of TERT and telomerase RNA required for catalytic activity and protein-RNA interaction for Tetrahymena thermophila telomerase. We found that the TERT amino and carboxyl termini, although evolutionarily poorly conserved, are nonetheless important for catalytic activity. In contrast, high-affinity telomerase RNA binding requires only a small region in the amino terminus of TERT. Surprisingly, the TERT region necessary and sufficient for telomerase RNA binding is completely separable from the reverse transcriptase motifs. The minimal Tetrahymena TERT RNA binding domain contains two sequence motifs with ciliate-specific conservation and one TERT motif with conservation across all species. With human TERT, we demonstrate that a similar region within the TERT amino terminus is essential for human telomerase RNA binding as well. Finally, we defined the Tetrahymena telomerase RNA sequences that are essential for TERT interaction. We found that a four-nucleotide region 5′ of the template is critical for TERT binding and that the 5′ end of telomerase RNA is sufficient for TERT binding. Our results reveal at least one evolutionarily conserved molecular mechanism by which the telomerase reverse transcriptase is functionally specialized for obligate use of an internal RNA template. American Society for Microbiology 2001-02 /pmc/articles/PMC99554/ /pubmed/11158287 http://dx.doi.org/10.1128/MCB.21.4.990-1000.2001 Text en Copyright © 2001, American Society for Microbiology
institution	US National Library of Medicine
collection	PubMed Central
language	en
format	Article
topic	DNA Dynamics and Chromosome Structure
spellingShingle	DNA Dynamics and Chromosome Structure Lai, Cary K. Mitchell, James R. Collins, Kathleen RNA Binding Domain of Telomerase Reverse Transcriptase
description	Telomerase is a ribonucleoprotein reverse transcriptase that extends the ends of chromosomes. The two telomerase subunits essential for catalysis in vitro are the telomerase reverse transcriptase (TERT) and the telomerase RNA. Using truncations and site-specific mutations, we identified sequence elements of TERT and telomerase RNA required for catalytic activity and protein-RNA interaction for Tetrahymena thermophila telomerase. We found that the TERT amino and carboxyl termini, although evolutionarily poorly conserved, are nonetheless important for catalytic activity. In contrast, high-affinity telomerase RNA binding requires only a small region in the amino terminus of TERT. Surprisingly, the TERT region necessary and sufficient for telomerase RNA binding is completely separable from the reverse transcriptase motifs. The minimal Tetrahymena TERT RNA binding domain contains two sequence motifs with ciliate-specific conservation and one TERT motif with conservation across all species. With human TERT, we demonstrate that a similar region within the TERT amino terminus is essential for human telomerase RNA binding as well. Finally, we defined the Tetrahymena telomerase RNA sequences that are essential for TERT interaction. We found that a four-nucleotide region 5′ of the template is critical for TERT binding and that the 5′ end of telomerase RNA is sufficient for TERT binding. Our results reveal at least one evolutionarily conserved molecular mechanism by which the telomerase reverse transcriptase is functionally specialized for obligate use of an internal RNA template.
author	Lai, Cary K. Mitchell, James R. Collins, Kathleen
author_facet	Lai, Cary K. Mitchell, James R. Collins, Kathleen
author_sort	Lai, Cary K.
title	RNA Binding Domain of Telomerase Reverse Transcriptase
title_short	RNA Binding Domain of Telomerase Reverse Transcriptase
title_full	RNA Binding Domain of Telomerase Reverse Transcriptase
title_fullStr	RNA Binding Domain of Telomerase Reverse Transcriptase
title_full_unstemmed	RNA Binding Domain of Telomerase Reverse Transcriptase
title_sort	rna binding domain of telomerase reverse transcriptase
publisher	American Society for Microbiology
publisher_facet	American Society for Microbiology
publishDate	2001
url	https://ncbi.nlm.nih.gov/pmc/articles/PMC99554/ https://ncbi.nlm.nih.gov/pubmed/11158287 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/MCB.21.4.990-1000.2001
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RNA Binding Domain of Telomerase Reverse Transcriptase

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