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  HOT1 is a mammalian direct telomere repeat-binding protein contributing to telomerase recruitment

Kappei, D., Butter, F., Benda, C., Scheibe, M., Draskovic, I., Stevense, M., et al. (2013). HOT1 is a mammalian direct telomere repeat-binding protein contributing to telomerase recruitment. EMBO JOURNAL, 32(12), 1681-1701. doi:10.1038/emboj.2013.105.

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 Creators:
Kappei, Dennis1, Author              
Butter, Falk2, Author              
Benda, Christian3, Author              
Scheibe, Marion2, Author              
Draskovic, Irena1, Author
Stevense, Michelle1, Author
Novo, Clara Lopes1, Author
Basquin, Claire3, Author              
Araki, Masatake1, Author
Araki, Kimi1, Author
Krastev, Dragomir Blazhev1, Author
Kittler, Ralf1, Author              
Jessberger, Rolf1, Author
Londono-Vallejo, J. Arturo1, Author
Mann, Matthias2, Author              
Buchholz, Frank1, Author              
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
3Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: HUMAN CANCER-CELLS; CAJAL BODIES; IN-VITRO; SATURATION MUTAGENESIS; DYSKERATOSIS-CONGENITA; AFFINITY PURIFICATION; HUMAN CST; LENGTH; POT1; RNADNA-protein interaction; HOT1; mass spectrometry; telomeres; telomere length;
 Abstract: Telomeres are repetitive DNA structures that, together with the shelterin and the CST complex, protect the ends of chromosomes. Telomere shortening is mitigated in stem and cancer cells through the de novo addition of telomeric repeats by telomerase. Telomere elongation requires the delivery of the telomerase complex to telomeres through a not yet fully understood mechanism. Factors promoting telomerase-telomere interaction are expected to directly bind telomeres and physically interact with the telomerase complex. In search for such a factor we carried out a SILAC-based DNA-protein interaction screen and identified HMBOX1, hereafter referred to as homeobox telomere-binding protein 1 (HOT1). HOT1 directly and specifically binds double-stranded telomere repeats, with the in vivo association correlating with binding to actively processed telomeres. Depletion and overexpression experiments classify HOT1 as a positive regulator of telomere length. Furthermore, immunoprecipitation and cell fractionation analyses show that HOT1 associates with the active telomerase complex and promotes chromatin association of telomerase. Collectively, these findings suggest that HOT1 supports telomerase-dependent telomere elongation.

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Language(s): eng - English
 Dates: 2013
 Publication Status: Published in print
 Pages: 21
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000320230600007
DOI: 10.1038/emboj.2013.105
 Degree: -

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Title: EMBO JOURNAL
Source Genre: Journal
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Publ. Info: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 32 (12) Sequence Number: - Start / End Page: 1681 - 1701 Identifier: ISSN: 0261-4189