ジャーナル: J Biol Chem / 年: 2016 タイトル: Molecular Architecture of Full-length TRF1 Favors Its Interaction with DNA. 著者: Jasminka Boskovic / Jaime Martinez-Gago / Marinela Mendez-Pertuz / Alberto Buscato / Jorge Luis Martinez-Torrecuadrada / Maria A Blasco / 要旨: 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.
照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.2 mm / 最大 デフォーカス(公称値): 3.5 µm / 倍率(公称値): 61350
試料ステージ
試料ホルダーモデル: SIDE ENTRY, EUCENTRIC
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画像解析
詳細
The selected images were normalized
粒子像選択
選択した数: 33106
CTF補正
ソフトウェア - 名称: CTFFIND (ver. 3)
初期モデル
モデルのタイプ: OTHER 詳細: The same initial model as for TRF1 apo structure and band passed TRF1 apo final volume were used as an initial model for TRF1-DNA reconstructruction