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-Structure paper
タイトル | Spatial Organization and Molecular Interactions of the Schizosaccharomyces pombe Ccq1-Tpz1-Poz1 Shelterin Complex. |
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ジャーナル・号・ページ | J Mol Biol, Vol. 429, Issue 19, Page 2863-2872, Year 2017 |
掲載日 | 2017年9月15日 |
著者 | Harry Scott / Jin-Kwang Kim / Clinton Yu / Lan Huang / Feng Qiao / Derek J Taylor / |
PubMed 要旨 | The shelterin complex is a macromolecular assembly of proteins that binds to and protects telomeric DNA, which composes the ends of all linear chromosomes. Shelterin proteins prevent chromosome ends ...The shelterin complex is a macromolecular assembly of proteins that binds to and protects telomeric DNA, which composes the ends of all linear chromosomes. Shelterin proteins prevent chromosome ends from fusing together and from eliciting erroneous induction of DNA damage response pathways. In addition, shelterin proteins play key roles in regulating the recruitment and activation of telomerase, an enzyme that extends telomeric DNA. In fission yeast, Schizosaccharomyces pombe, interactions between the shelterin proteins Ccq1, Tpz1, and Poz1 are important for regulating telomerase-mediated telomere synthesis and thus telomere length homeostasis. Here, we used electron microscopy combined with genetic labeling to define the three-dimensional arrangement of the S. pombe Ccq1-Tpz1-Poz1 (CTP) complex. Crosslinking mass spectrometry was used to identify individual residues that are in proximity to the protein-protein interfaces of the assembled CTP complex. Together, our data provide a first glimpse into the architectural design of the CTP complex and reveals unique interactions that are important in maintaining the S. pombe telomere in a non-extendible state. |
リンク | J Mol Biol / PubMed:28807855 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 25.9 - 34.4 Å |
構造データ | EMDB-8863: EMDB-8864: EMDB-8865: EMDB-8866: |
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