NDLI: TIN2-Tethered TPP1 Recruits Human Telomerase to Telomeres In Vivo ▿

Content Provider	PubMed Central
Author	Abreu, Eladio Elena, Aritonovska Reichenbach, Patrick Cristofari, Gaël Culp, Brad Terns, Rebecca M. Lingner, Joachim Terns, Michael P.
Copyright Year	2010
Abstract	Recruitment to telomeres is a pivotal step in the function and regulation of human telomerase; however, the molecular basis for recruitment is not known. Here, we have directly investigated the process of telomerase recruitment via fluorescence in situ hybridization (FISH) and chromatin immunoprecipitation (ChIP). We find that depletion of two components of the shelterin complex that is found at telomeres—TPP1 and the protein that tethers TPP1 to the complex, TIN2—results in a loss of telomerase recruitment. On the other hand, we find that the majority of the observed telomerase association with telomeres does not require POT1, the shelterin protein that links TPP1 to the single-stranded region of the telomere. Deletion of the oligonucleotide/oligosaccharide binding fold (OB-fold) of TPP1 disrupts telomerase recruitment. In addition, while loss of TPP1 results in the appearance of DNA damage factors at telomeres, the DNA damage response per se does not account for the telomerase recruitment defect observed in the absence of TPP1. Our findings indicate that TIN2-anchored TPP1 plays a major role in the recruitment of telomerase to telomeres in human cells and that recruitment does not depend on POT1 or interaction of the shelterin complex with the single-stranded region of the telomere.
Related Links	http://dx.doi.org/10.1128/mcb.00240-10
Ending Page	2982
Page Count	12
Starting Page	2971
File Format	PDF
ISSN	02707306
e-ISSN	10985549
Journal	Molecular and Cellular Biology
Issue Number	12
Volume Number	30
Language	English
Publisher	American Society for Microbiology (ASM)
Publisher Date	2010-06-15
Access Restriction	Open
Rights Holder	American Society for Microbiology (ASM)
Subject Keyword	Cell Biology Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

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