TRFH domain: at the root of telomere protein evolution?

Giraud-Panis, Marie-Josèphe; Ye, Jing; Gilson, Éric

doi:10.1038/cr.2017.152

Cited by 10 publications

(3 citation statements)

References 12 publications

(14 reference statements)

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“…Conversely, SLX4 binds to the TRF homology (TRFH) domain of TRF2 ( Wan et al, 2013 ). The TRFH domain is a versatile docking site for various partner proteins ( Giraud-Panis et al, 2018 ). The crystal structure of the SLX4 TBM -TRF2 TRFH complex shows that SLX4 TBM adopts an extended conformation with a short one-turn helix at the N-terminus and fits neatly into a narrow groove formed by the TRF2 TRFH ( Figure 5D ) ( Wan et al, 2013 ).…”

Section: Slx1-slx4 Has Pivotal Roles In Dna Repair and Genome Stabilitymentioning

confidence: 99%

Exploring the Structures and Functions of Macromolecular SLX4-Nuclease Complexes in Genome Stability

et al. 2021

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All organisms depend on the ability of cells to accurately duplicate and segregate DNA into progeny. However, DNA is frequently damaged by factors in the environment and from within cells. One of the most dangerous lesions is a DNA double-strand break. Unrepaired breaks are a major driving force for genome instability. Cells contain sophisticated DNA repair networks to counteract the harmful effects of genotoxic agents, thus safeguarding genome integrity. Homologous recombination is a high-fidelity, template-dependent DNA repair pathway essential for the accurate repair of DNA nicks, gaps and double-strand breaks. Accurate homologous recombination depends on the ability of cells to remove branched DNA structures that form during repair, which is achieved through the opposing actions of helicases and structure-selective endonucleases. This review focuses on a structure-selective endonuclease called SLX1-SLX4 and the macromolecular endonuclease complexes that assemble on the SLX4 scaffold. First, we discuss recent developments that illuminate the structure and biochemical properties of this somewhat atypical structure-selective endonuclease. We then summarize the multifaceted roles that are fulfilled by human SLX1-SLX4 and its associated endonucleases in homologous recombination and genome stability. Finally, we discuss recent work on SLX4-binding proteins that may represent integral components of these macromolecular nuclease complexes, emphasizing the structure and function of a protein called SLX4IP.

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Section: Slx1-slx4 Has Pivotal Roles In Dna Repair and Genome Stabilitymentioning

confidence: 99%

Exploring the Structures and Functions of Macromolecular SLX4-Nuclease Complexes in Genome Stability

et al. 2021

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“…Shelterin proteins form bridged telomeric protein complexes and are involved in many telomeric functions like telomerase regulation, protection against activation of the DNA damage response, chromosome stability, long and short range transcriptional regulation and meiosis 12 . The shelterin complex is usually composed of both single-stand and double-strand telomeric DNA binding proteins as well as other proteins bridging them.…”

Section: Introductionmentioning

confidence: 99%

Unzipped genome assemblies of polyploid root-knot nematodes reveal new kinds of unilateral composite telomeric repeats

Danchin

Mota

Koutsovoulos

et al. 2023

Preprint

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Using long read sequencing we have assembled and unzipped the genomes of Meloidogyne incognita, M. javanica and M. arenaria, the three most devastating plant-parasitic nematodes at unparalleled contiguity. The telomeric repeat (TTAGGC)n, evolutionarily conserved in nematodes, was not found in these genomes. Furthermore, no evidence for a telomerase enzyme or for orthologs of C. elegans telomere-associated proteins could be found. Instead, we identified species-specific composite repeats enriched at one extremity of contigs. These repeats were G-rich, oriented and transcribed, similarly to known telomeric repeats. Using fluorescent in situ hybridization, we confirmed these repeats had telomeric location at one single end of M. incognita chromosomes. The discovery of a new kind of telomeric repeat in these species highlights the evolutionary diversity of chromosome protection systems despite their central roles in senescence, aging and chromosome integrity and opens new perspectives towards the development of more specific control methods against these pests.

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“…Humans have evolved a more elaborate system containing 6 proteins (TRF1, TRF2, RAP1, TIN2, TPP1 and POT1) but the ultimate goal remains the same: inhibiting activation of the DNA damage response (DDR) and double strand break (DSB) repair as well as recruiting/regulating the telomerase, an enzyme that elongates telomeres. Despite overall differences in composition, common structural themes can be found: Myb/SANT (Telobox) domains for specific binding to double stranded telomeric DNA repeats ( 5 ), oligonucleotide/oligosaccharide binding (OB) folds for binding the single stranded telomeric DNA repeats and TRFH domains for protein and additional DNA interactions ( 6 ). Protecting telomeres termini from DNA damage signaling and repair is a major role of TRF2 ( 7 ).…”

Section: Introductionmentioning

confidence: 99%

The non-telomeric evolutionary trajectory of TRF2 in zebrafish reveals its specific roles in neurodevelopment and aging

Ying

Han

et al. 2022

Nucleic Acids Research

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The shelterin protein complex is required for telomere protection in various eukaryotic organisms. In mammals, the shelterin subunit TRF2 is specialized in preventing ATM activation at telomeres and chromosome end fusion in somatic cells. Here, we demonstrate that the zebrafish ortholog of TRF2 (encoded by the terfa gene) is protecting against unwanted ATM activation genome-wide. The terfa-compromised fish develop a prominent and specific embryonic neurodevelopmental failure. The heterozygous fish survive to adulthood but exhibit a premature aging phenotype. The recovery from embryonic neurodevelopmental failure requires both ATM inhibition and transcriptional complementation of neural genes. Furthermore, restoring the expression of TRF2 in glial cells rescues the embryonic neurodevelopment phenotype. These results indicate that the shelterin subunit TRF2 evolved in zebrafish as a general factor of genome maintenance and transcriptional regulation that is required for proper neurodevelopment and normal aging. These findings uncover how TRF2 links development to aging by separate functions in gene expression regulation and genome stability control.

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TRFH domain: at the root of telomere protein evolution?

Cited by 10 publications

References 12 publications

Exploring the Structures and Functions of Macromolecular SLX4-Nuclease Complexes in Genome Stability

Exploring the Structures and Functions of Macromolecular SLX4-Nuclease Complexes in Genome Stability

Unzipped genome assemblies of polyploid root-knot nematodes reveal new kinds of unilateral composite telomeric repeats

The non-telomeric evolutionary trajectory of TRF2 in zebrafish reveals its specific roles in neurodevelopment and aging

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