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PMID: 15632080 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Human protection of telomeres 1 (POT1) is a negative regulator of telomerase activity in vitro.

Molecular and cellular biology ·Vol. 25 ·No. 2 ·2005-01-00 ·Pages 808-18

Kelleher C, Kurth I, Lingner J

Abstract

The telomeric single-strand DNA binding protein protection of telomeres 1 (POT1) protects telomeres from rapid degradation in Schizosaccharomyces pombe and has been implicated in positive and negative telomere length regulation in humans. Human POT1 appears to interact with telomeres both through direct binding to the 3' overhanging G-strand DNA and through interaction with the TRF1 duplex telomere DNA binding complex. The influence of POT1 on telomerase activity has not been studied at the molecular level. We show here that POT1 negatively effects telomerase activity in vitro. We find that the DNA binding activity of POT1 is required for telomerase inhibition. Furthermore, POT1 is incapable of inhibiting telomeric repeat addition to substrate primers that are defective for POT1 binding, suggesting that in vivo, POT1 likely affects substrate access to telomerase.

MeSH Terms
Animals Binding Sites DNA, Single-Stranded/metabolism DNA-Binding Proteins/genetics,metabolism HeLa Cells Humans Protein Binding Protein Structure, Tertiary Shelterin Complex Telomerase/antagonists & inhibitors,genetics,metabolism Telomere/metabolism Telomere-Binding Proteins/genetics,metabolism
Chemicals
DNA, Single-Stranded DNA-Binding Proteins POT1 protein, human Shelterin Complex Telomere-Binding Proteins Telomerase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kelleher Colleen
ISREC, Chemin des Boveresses 155, 1066 Epalinges, Switzerland.
Kurth Isabel
Lingner Joachim
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
2005-01-00
Pages
808-18
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC543404
Subset
IM
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