Open Access

Nature, volume 492, issue 7428, pages 285-289

The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity

Nandakumar Jayakrishnan ^{1, 2}

Bell Caitlin F ^{1, 2, 3}

Weidenfeld Ina ^{1, 4}

Zaug Arthur J ^{1, 2}

Leinwand Leslie A ^{1, 4}

Cech Thomas R ^{1, 2, 4}

Hide authors affiliations Show authors affiliations: 4 affiliations

University of Colorado BioFrontiers Institute, Boulder, Colorado 80309, USA, |

Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Colorado, Boulder, USA |

Present address: Vanderbilt School of Medicine, M.D. program, 215 Light Hall, Nashville, Tennessee 37232, USA., |

⁴

Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, USA |

Publication type: Journal Article

Publication date: 2012-10-24

Springer Nature

Journal: Nature

Quartile SCImago

Quartile WOS

Impact factor: 64.8

ISSN: 00280836, 14764687

DOI: 10.1038/nature11648

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PubMed ID: 23103865

Multidisciplinary

Abstract

Human chromosome ends are capped by shelterin, a protein complex that protects the natural ends from being recognized as sites of DNA damage and also regulates the telomere-replicating enzyme, telomerase. Shelterin includes the heterodimeric POT1–TPP1 protein, which binds the telomeric single-stranded DNA tail. TPP1 has been implicated both in recruiting telomerase to telomeres and in stimulating telomerase processivity (the addition of multiple DNA repeats after a single primer-binding event). Determining the mechanisms of these activities has been difficult, especially because genetic perturbations also tend to affect the essential chromosome end-protection function of TPP1 (refs 15, 16, 17). Here we identify separation-of-function mutants of human TPP1 that retain full telomere-capping function in vitro and in vivo, yet are defective in binding human telomerase. The seven separation-of-function mutations map to a patch of amino acids on the surface of TPP1, the TEL patch, that both recruits telomerase to telomeres and promotes high-processivity DNA synthesis, indicating that these two activities are manifestations of the same molecular interaction. Given that the interaction between telomerase and TPP1 is required for telomerase function in vivo, the TEL patch of TPP1 provides a new target for anticancer drug development.

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Citations by publishers

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Springer Nature	Springer Nature, 52, 18.71% Springer Nature 52 publications, 18.71%
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S. Karger AG	S. Karger AG, 1, 0.36% S. Karger AG 1 publication, 0.36%
Portland Press	Portland Press, 1, 0.36% Portland Press 1 publication, 0.36%
Wolters Kluwer Health	Wolters Kluwer Health, 1, 0.36% Wolters Kluwer Health 1 publication, 0.36%
Higher Education Press	Higher Education Press, 1, 0.36% Higher Education Press 1 publication, 0.36%
IOP Publishing	IOP Publishing, 1, 0.36% IOP Publishing 1 publication, 0.36%
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Pleiades Publishing	Pleiades Publishing, 1, 0.36% Pleiades Publishing 1 publication, 0.36%
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GOST Copy

Nandakumar J. et al. The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity // Nature. 2012. Vol. 492. No. 7428. pp. 285-289.

GOST all authors (up to 50) Copy

Nandakumar J., Bell C. F., Weidenfeld I., Zaug A. J., Leinwand L. A., Cech T. R. The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity // Nature. 2012. Vol. 492. No. 7428. pp. 285-289.

RIS |

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RIS Copy

TY - JOUR

DO - 10.1038/nature11648

UR - https://doi.org/10.1038%2Fnature11648

TI - The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity

T2 - Nature

AU - Nandakumar, Jayakrishnan

AU - Bell, Caitlin F

AU - Weidenfeld, Ina

AU - Zaug, Arthur J

AU - Leinwand, Leslie A

AU - Cech, Thomas R

PY - 2012

DA - 2012/10/24 00:00:00

PB - Springer Nature

SP - 285-289

IS - 7428

VL - 492

PMID - 23103865

SN - 0028-0836

SN - 1476-4687

ER -

BibTex |

Cite this

BibTex Copy

@article{2012_Nandakumar,

author = {Jayakrishnan Nandakumar and Caitlin F Bell and Ina Weidenfeld and Arthur J Zaug and Leslie A Leinwand and Thomas R Cech},

title = {The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity},

journal = {Nature},

year = {2012},

volume = {492},

publisher = {Springer Nature},

month = {oct},

url = {https://doi.org/10.1038%2Fnature11648},

number = {7428},

pages = {285--289},

doi = {10.1038/nature11648}

}

MLA

Cite this

MLA Copy

Nandakumar, Jayakrishnan, et al. “The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity.” Nature, vol. 492, no. 7428, Oct. 2012, pp. 285-289. https://doi.org/10.1038%2Fnature11648.

Found error?

Publisher

Springer Nature

Journal

Nature

Quartile SCImago

Quartile WOS

Impact factor

64.8

ISSN

00280836 (Print)
14764687 (Electronic)