EMD-8865

Single-particle
30.7 Å
EMD-8865 Deposition: 28/07/2017
Map released: 08/11/2017
Last modified: 14/02/2018
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-8865

Negative-stain reconstruction of an N-terminally MBP tagged Poz1 in the S. pombe CTP complex (Ccq1 2-716, Tpz1 406-508, Poz1 2-249)

EMD-8865

Single-particle
30.7 Å
EMD-8865 Deposition: 28/07/2017
Map released: 08/11/2017
Last modified: 14/02/2018
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Schizosaccharomyces pombe
Sample: Negative-stain reconstruction of an N-terminally MBP tagged Poz1 in the S. pombe CTP complex (Ccq1 2-716, Tpz1 406-508, Poz1 2-249)

Deposition Authors: Scott HW, Kim JK, Yu C, Huang L, Qiao F, Taylor DJ
Spatial Organization and Molecular Interactions of the Schizosaccharomyces pombe Ccq1-Tpz1-Poz1 Shelterin Complex.
Scott H, Kim JK, Yu C, Huang L, Qiao F, Taylor DJ
(2017) J. Mol. Biol. , 429 , 2863 - 2872
PUBMED: 28807855
DOI: doi:10.1016/j.jmb.2017.08.002
ISSN: 1089-8638
ASTM: JMOBAK
Abstract:
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.