Fission yeast telomere-binding protein Taz1 is a functional but not a structural counterpart of human TRF1 and TRF2

Deng, Wei; Wu, Jian; Wang, Feng; Kanoh, Junko; Dehé, Pierre-Marie; Chen, Juan; Lei, Ming

doi:10.1038/cr.2015.76

Cited by 18 publications

(27 citation statements)

References 15 publications

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“…The S. pombe homolog of human TRF1 and TRF2, Taz1, also contains an α-helical domain that has been considered as the TRFH domain of Taz1 [10,20,50] ( Figure 6A). Our previous structural studies confirmed that Taz1 TRFH indeed exhibits similar topological architecture to the TRFH domains of human TRF proteins [48] ( Figure 6A). Consistently, pairwise structural comparison showed that Poz1 is also structurally similar to Taz1 TRFH with an r.m.s.d.…”

Section: Structural Resemblance Of Poz1 To Other Telomere Proteinssupporting

confidence: 69%

“…The α-helical architecture of Poz1 prompted us to investigate the structural relationship between Poz1 and other telomere proteins with domains of α-helical architecture -the TRFH domains of human TRF1 and TRF2 and S. pombe Taz1 [36,48,49] (Figure 6A). Pairwise structural analysis revealed an unequivocal structural similarity of Poz1 to other TRFH domains (Supplementary information, Figure S11).…”

Section: Structural Resemblance Of Poz1 To Other Telomere Proteinsmentioning

confidence: 99%

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Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex

Xue

Chen

et al. 2017

Cell Res

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Telomeric shelterin complex caps chromosome ends and plays a crucial role in telomere maintenance and protection. In the fission yeast Schizosaccharomyces pombe, shelterin is composed of telomeric single- and double-stranded DNA-binding protein subcomplexes Pot1-Tpz1 and Taz1-Rap1, which are bridged by their interacting protein Poz1. However, the structure of Poz1 and how Poz1 functions as an interaction hub in the shelterin complex remain unclear. Here we report the crystal structure of Poz1 in complex with Poz1-binding motifs of Tpz1 and Rap1. The crystal structure shows that Poz1 employs two different binding surfaces to interact with Tpz1 and Rap1. Unexpectedly, the structure also reveals that Poz1 adopts a dimeric conformation. Mutational analyses suggest that proper interactions between Tpz1, Poz1, and Rap1 in the shelterin core complex are required for telomere length homeostasis and heterochromatin structure maintenance at telomeres. Structural resemblance between Poz1 and the TRFH domains of other shelterin proteins in fission yeast and humans suggests a model for the evolution of shelterin proteins.

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Section: Structural Resemblance Of Poz1 To Other Telomere Proteinssupporting

confidence: 69%

Section: Structural Resemblance Of Poz1 To Other Telomere Proteinsmentioning

confidence: 99%

Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex

Xue

Chen

et al. 2017

Cell Res

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“…The double-stranded DNA-binding proteins, including TRF1 and TRF2 in mammals and Taz1 in fission yeast, predominantly bind telomere DNA as preformed homodimers to maintain proper telomere length [29,30]. Mutations that abrogate S. pombe Taz1 dimerization result in a 10-fold decrease in telomeric DNA-binding in vitro and fail to associate with telomeres in vivo [31]. As a result, the dimerization-deficient taz1 mutant cells bear heterogeneously elongated telomeres, similar to those in taz1 Δ cells, thereby punctuating the critical role of Taz1 dimerization in regulating telomere length.…”

Section: Discussionmentioning

confidence: 99%

Spatial Organization and Molecular Interactions of the Schizosaccharomyces pombe Ccq1–Tpz1–Poz1 Shelterin Complex

Scott

Kim

et al. 2017

Journal of Molecular Biology

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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. Additionally, 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. Cross-linking 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.

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“…In both fission yeast and mammalian cells, spatial and temporal regulation of DNA replication was almost completely abrogated in rif1∆ cells (Cornacchia et al, 2012;Hayano et al, 2012;Yamazaki et al, 2012Yamazaki et al, , 2013. Taz1 is another telomere-binding protein in fission yeast (an ortholog of human TRF1/TRF2 with a DNA-binding Myb domain; Cooper et al, 1997;Deng et al, 2015). Telomeres are elongated in taz1∆ cells.…”

Section: Introductionmentioning

confidence: 99%

Telomere-binding factors in the regulation of DNA replication

et al. 2017

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Recent studies have indicated new roles for telomere-binding factors in the regulation of DNA replication, not only at the telomeres but also at the arm regions of the chromosome. Among these factors, Rif1, a conserved protein originally identified in yeasts as a telomere regulator, plays a major role in the spatiotemporal regulation of DNA replication during S phase. Its ability to interact with phosphatases and to create specific higher-order chromatin structures is central to the mechanism by which Rif1 exerts this function. In this review, we discuss recent progress in elucidating the roles of Rif1 and other telomere-binding factors in the regulation of chromosome events occurring at locations other than telomeres.

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Fission yeast telomere-binding protein Taz1 is a functional but not a structural counterpart of human TRF1 and TRF2

Cited by 18 publications

References 15 publications

Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex

Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex

Spatial Organization and Molecular Interactions of the Schizosaccharomyces pombe Ccq1–Tpz1–Poz1 Shelterin Complex

Telomere-binding factors in the regulation of DNA replication

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