Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase

Maintenance of telomere integrity requires the dynamic interplay between telomerase, telomere-associated proteins and DNA repair proteins. These interactions are vital to suppress DNA damage responses and changes in chromosome dynamics that can result in aneuploidy or other transforming aberrations....

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Main Authors:	Ting, Nicholas S. Y., Yu, Yaping, Pohorelic, Brant, Lees-Miller, Susan P., Beattie, Tara L.
Format:	Online
Language:	English
Published:	Oxford University Press 2005
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1075923/

id	pubmed-1075923
recordtype	oai_dc
spelling	pubmed-10759232005-04-11 Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase Ting, Nicholas S. Y. Yu, Yaping Pohorelic, Brant Lees-Miller, Susan P. Beattie, Tara L. Article Maintenance of telomere integrity requires the dynamic interplay between telomerase, telomere-associated proteins and DNA repair proteins. These interactions are vital to suppress DNA damage responses and changes in chromosome dynamics that can result in aneuploidy or other transforming aberrations. The interaction between the DNA repair protein Ku and the RNA component of telomerase (TLC1) in Saccharomyces cerevisiae has been shown to be important for maintaining telomere length. Here, we sought to determine whether this interaction was conserved in higher eukaryotes. Although there is no sequence similarity between TLC1 and the RNA component (hTR) of human telomerase, we show that human Ku70/80 interacts with hTR both in vitro and in a cellular context. Specifically, Ku70/80 interacts with a 47 nt region of the 3′ end of hTR, which resembles the stem–loop region of the yeast Ku70/80 binding domain on TLC1. Furthermore, utilizing immunoprecipitation/RT–PCR experiments, we show that Ku interacts with hTR in cell lines deficient in the human telomerase reverse transcriptase protein (hTERT), suggesting that this interaction does not require hTERT. These data suggest that Ku interacts directly with hTR, independent of hTERT, providing evidence for the conservation of the interaction between Ku and telomerase RNA among various species and provide significant insight into how Ku is involved in telomere maintenance in higher eukaryotes. Oxford University Press 2005 2005-04-11 /pmc/articles/PMC1075923/ /pubmed/15824061 http://dx.doi.org/10.1093/nar/gki342 Text en © The Author 2005. Published by Oxford University Press. All rights reserved
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Ting, Nicholas S. Y. Yu, Yaping Pohorelic, Brant Lees-Miller, Susan P. Beattie, Tara L.
spellingShingle	Ting, Nicholas S. Y. Yu, Yaping Pohorelic, Brant Lees-Miller, Susan P. Beattie, Tara L. Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase
author_facet	Ting, Nicholas S. Y. Yu, Yaping Pohorelic, Brant Lees-Miller, Susan P. Beattie, Tara L.
author_sort	Ting, Nicholas S. Y.
title	Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase
title_short	Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase
title_full	Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase
title_fullStr	Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase
title_full_unstemmed	Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase
title_sort	human ku70/80 interacts directly with htr, the rna component of human telomerase
description	Maintenance of telomere integrity requires the dynamic interplay between telomerase, telomere-associated proteins and DNA repair proteins. These interactions are vital to suppress DNA damage responses and changes in chromosome dynamics that can result in aneuploidy or other transforming aberrations. The interaction between the DNA repair protein Ku and the RNA component of telomerase (TLC1) in Saccharomyces cerevisiae has been shown to be important for maintaining telomere length. Here, we sought to determine whether this interaction was conserved in higher eukaryotes. Although there is no sequence similarity between TLC1 and the RNA component (hTR) of human telomerase, we show that human Ku70/80 interacts with hTR both in vitro and in a cellular context. Specifically, Ku70/80 interacts with a 47 nt region of the 3′ end of hTR, which resembles the stem–loop region of the yeast Ku70/80 binding domain on TLC1. Furthermore, utilizing immunoprecipitation/RT–PCR experiments, we show that Ku interacts with hTR in cell lines deficient in the human telomerase reverse transcriptase protein (hTERT), suggesting that this interaction does not require hTERT. These data suggest that Ku interacts directly with hTR, independent of hTERT, providing evidence for the conservation of the interaction between Ku and telomerase RNA among various species and provide significant insight into how Ku is involved in telomere maintenance in higher eukaryotes.
publisher	Oxford University Press
publishDate	2005
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1075923/
_version_	1611373237462106112

Human Ku70/80 interacts directly with hTR, the RNA component of human telomerase

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