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TitleMolecular Architecture of Full-length TRF1 Favors Its Interaction with DNA.
Journal, issue, pagesJ Biol Chem, Vol. 291, Issue 41, Page 21829-21835, Year 2016
Publish dateOct 7, 2016
AuthorsJasminka Boskovic / Jaime Martinez-Gago / Marinela Mendez-Pertuz / Alberto Buscato / Jorge Luis Martinez-Torrecuadrada / Maria A Blasco /
PubMed AbstractTelomeres are specific DNA-protein structures found at both ends of eukaryotic chromosomes that protect the genome from degradation and from being recognized as double-stranded breaks. In ...Telomeres are specific DNA-protein structures found at both ends of eukaryotic chromosomes that protect the genome from degradation and from being recognized as double-stranded breaks. In vertebrates, telomeres are composed of tandem repeats of the TTAGGG sequence that are bound by a six-subunit complex called shelterin. Molecular mechanisms of telomere functions remain unknown in large part due to lack of structural data on shelterins, shelterin complex, and its interaction with the telomeric DNA repeats. TRF1 is one of the best studied shelterin components; however, the molecular architecture of the full-length protein remains unknown. We have used single-particle electron microscopy to elucidate the structure of TRF1 and its interaction with telomeric DNA sequence. Our results demonstrate that full-length TRF1 presents a molecular architecture that assists its interaction with telometic DNA and at the same time makes TRFH domains accessible to other TRF1 binding partners. Furthermore, our studies suggest hypothetical models on how other proteins as TIN2 and tankyrase contribute to regulate TRF1 function.
External linksJ Biol Chem / PubMed:27563064 / PubMed Central
MethodsEM (single particle)
Resolution23.0 - 25.0 Å
Structure data

EMDB-4105:
TRF1 apo
Method: EM (single particle) / Resolution: 23.0 Å

EMDB-4106:
TRF1-DNA
Method: EM (single particle) / Resolution: 25.0 Å

Source
  • Mus musculus (house mouse)

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