Human Ku70/80 associates physically with telomerase through interaction with hTERT

Weihang Chai; Lance P Ford; Lisa Lenertz; Woodring E Wright; Jerry W Shay

doi:10.1074/jbc.M208542200

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Human Ku70/80 associates physically with telomerase through interaction with hTERT

Journal article

Open access

Peer reviewed

Human Ku70/80 associates physically with telomerase through interaction with hTERT

Weihang Chai, Lance P Ford, Lisa Lenertz, Woodring E Wright and Jerry W Shay

The Journal of biological chemistry, Vol.277(49), pp.47242-47247

12/06/2002

DOI: https://doi.org/10.1074/jbc.M208542200

Handle:

https://hdl.handle.net/2376/110573

PMID: 12377759

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Abstract

Catalytic Domain

Humans

Nuclear Proteins - metabolism

Nuclear Proteins - chemistry

DNA-Binding Proteins - chemistry

Plasmids - metabolism

Precipitin Tests

DNA-Binding Proteins - metabolism

DNA Helicases

Antigens, Nuclear

Ku Autoantigen

Telomerase - chemistry

Protein Binding

Telomerase - metabolism

Telomere - metabolism

Tumor Cells, Cultured

DNA, Complementary - metabolism

Fibroblasts - metabolism

Telomere length maintenance, an activity essential for chromosome stability and genome integrity, is regulated by telomerase- and telomere-associated factors. The DNA repair protein Ku (a heterodimer of Ku70 and Ku80 subunits) associates with mammalian telomeres and contributes to telomere maintenance. Here, we analyzed the physical association of Ku with human telomerase both in vivo and in vitro. Antibodies specific to human Ku proteins precipitated human telomerase in extracts from tumor cells, as well as from telomerase-immortalized normal cells, regardless of the presence of DNA-dependent protein kinase catalytic subunit. The same Ku antibodies also precipitated in vitro reconstituted telomerase, suggesting that this association does not require telomeric DNA. Moreover, Ku associated with the in vitro translated catalytic subunit of telomerase (hTERT) in the absence of telomerase RNA (hTR) or telomeric DNA. The results presented here are the first to report that Ku associates with hTERT, and this interaction may function to regulate the access of telomerase to telomeric DNA ends.

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Title: Human Ku70/80 associates physically with telomerase through interaction with hTERT
Creators: Weihang Chai - Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9039, USA
Lance P Ford
Lisa Lenertz
Woodring E Wright
Jerry W Shay
Publication Details: The Journal of biological chemistry, Vol.277(49), pp.47242-47247
Academic Unit: UNKNOWN
Publisher: United States
Grant note: AG01228 / NIA NIH HHS
Identifiers: 99900547048501842
Language: English
Resource Type: Journal article