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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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Kappei, Dennis1, Autor           
Butter, Falk2, Autor           
Benda, Christian3, Autor           
Scheibe, Marion2, Autor           
Draskovic, Irena1, Autor
Stevense, Michelle1, Autor
Novo, Clara Lopes1, Autor
Basquin, Claire3, Autor           
Araki, Masatake1, Autor
Araki, Kimi1, Autor
Krastev, Dragomir Blazhev1, Autor
Kittler, Ralf1, Autor           
Jessberger, Rolf1, Autor
Londono-Vallejo, J. Arturo1, Autor
Mann, Matthias2, Autor           
Buchholz, Frank1, Autor           
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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Schlagwörter: 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;
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2013
 Publikationsstatus: Erschienen
 Seiten: 21
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000320230600007
DOI: 10.1038/emboj.2013.105
 Art des Abschluß: -

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Titel: EMBO JOURNAL
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Seiten: - Band / Heft: 32 (12) Artikelnummer: - Start- / Endseite: 1681 - 1701 Identifikator: ISSN: 0261-4189