Journal: J Biol Chem / Year: 2016 Title: Molecular Architecture of Full-length TRF1 Favors Its Interaction with DNA. Authors: Jasminka Boskovic / Jaime Martinez-Gago / Marinela Mendez-Pertuz / Alberto Buscato / Jorge Luis Martinez-Torrecuadrada / Maria A Blasco / Abstract: 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 ...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.
History
Deposition
Aug 23, 2016
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Header (metadata) release
Sep 7, 2016
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Map release
Sep 7, 2016
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Update
Aug 2, 2017
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Current status
Aug 2, 2017
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Type: NEGATIVE / Material: Uranyl Acetate Details: Nagatively stained images were prepared using standard 1% Uranyl-acetate staining procedure
Grid
Model: Electron Microscopy SciencesCF400-CU / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR
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Electron microscopy
Microscope
FEI TECNAI 12
Image recording
Film or detector model: TVIPS TEMCAM-F416 (4k x 4k) / Digitization - Sampling interval: 15.6 µm / Number grids imaged: 1 / Average exposure time: 1.0 sec. / Average electron dose: 15.0 e/Å2
Electron beam
Acceleration voltage: 120 kV / Electron source: LAB6
Number selected: 32880 Details: We have used eider semi-automatic particle selection implemented in EMAN2 or manual particle selection implemented in EMAN1
CTF correction
Software - Name: CTFFIND (ver. 3)
Startup model
Type of model: OTHER Details: We used reference free 2D averages as intup into the program e2initialmodel.py implemented in EMAN2 with C2 symmetry
Final reconstruction
Applied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 23.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: Xmipp (ver. 2.4) / Number images used: 10769
Initial angle assignment
Type: PROJECTION MATCHING / Software - Name: EMAN (ver. 1.9)
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