The G-quadruplex ligand telomestatin impairs binding of topoisomerase IIIalpha to G-quadruplex-forming oligonucleotides and uncaps telomeres in ALT cells. Temime-Smaali, N., Guittat, L., Sidibe, A., Shin-ya, K., Trentesaux, C., & Riou, J. PloS one, 4(9):e6919, January, 2009. ![The G-quadruplex ligand telomestatin impairs binding of topoisomerase IIIalpha to G-quadruplex-forming oligonucleotides and uncaps telomeres in ALT cells. [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex In Alternative Lengthening of Telomeres (ALT) cell lines, specific nuclear bodies called APBs (ALT-associated PML bodies) concentrate telomeric DNA, shelterin components and recombination factors associated with telomere recombination. Topoisomerase IIIalpha (Topo III) is an essential telomeric-associated factor in ALT cells. We show here that the binding of Topo III to telomeric G-overhang is modulated by G-quadruplex formation. Topo III binding to G-quadruplex-forming oligonucleotides was strongly inhibited by telomestatin, a potent and specific G-quadruplex ligand. In ALT cells, telomestatin treatment resulted in the depletion of the Topo III/BLM/TRF2 complex and the disruption of APBs and led to the segregation of PML, shelterin components and Topo III. Interestingly, a DNA damage response was observed at telomeres in telomestatin-treated cells. These data indicate the importance of G-quadruplex stabilization during telomere maintenance in ALT cells. The function of TRF2/Topo III/BLM in the resolution of replication intermediates at telomeres is discussed.
@article{temime-smaali_g-quadruplex_2009,
title = {The {G}-quadruplex ligand telomestatin impairs binding of topoisomerase {IIIalpha} to {G}-quadruplex-forming oligonucleotides and uncaps telomeres in {ALT} cells.},
volume = {4},
issn = {1932-6203},
url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2732903&tool=pmcentrez&rendertype=abstract},
doi = {10.1371/journal.pone.0006919},
abstract = {In Alternative Lengthening of Telomeres (ALT) cell lines, specific nuclear bodies called APBs (ALT-associated PML bodies) concentrate telomeric DNA, shelterin components and recombination factors associated with telomere recombination. Topoisomerase IIIalpha (Topo III) is an essential telomeric-associated factor in ALT cells. We show here that the binding of Topo III to telomeric G-overhang is modulated by G-quadruplex formation. Topo III binding to G-quadruplex-forming oligonucleotides was strongly inhibited by telomestatin, a potent and specific G-quadruplex ligand. In ALT cells, telomestatin treatment resulted in the depletion of the Topo III/BLM/TRF2 complex and the disruption of APBs and led to the segregation of PML, shelterin components and Topo III. Interestingly, a DNA damage response was observed at telomeres in telomestatin-treated cells. These data indicate the importance of G-quadruplex stabilization during telomere maintenance in ALT cells. The function of TRF2/Topo III/BLM in the resolution of replication intermediates at telomeres is discussed.},
number = {9},
journal = {PloS one},
author = {Temime-Smaali, Nassima and Guittat, Lionel and Sidibe, Assitan and Shin-ya, Kazuo and Trentesaux, Chantal and Riou, Jean-François},
month = jan,
year = {2009},
pmid = {19742304},
keywords = {\#nosource, Biological, Cell Nucleus, Cell Nucleus: metabolism, Cell Separation, Cells, Cultured, DNA Topoisomerases, Flow Cytometry, G-Quadruplexes, Genetic, Humans, Ligands, Models, Oligonucleotides, Oligonucleotides: chemistry, Oxazoles, Oxazoles: metabolism, Protein Binding, Protein Structure, Recombination, Telomere, Telomere: metabolism, Telomere: ultrastructure, Tertiary, Type I, Type I: metabolism},
pages = {e6919},
}
Downloads: 0
{"_id":"yYwiPsnHBK8Xi3ph2","bibbaseid":"temimesmaali-guittat-sidibe-shinya-trentesaux-riou-thegquadruplexligandtelomestatinimpairsbindingoftopoisomeraseiiialphatogquadruplexformingoligonucleotidesanduncapstelomeresinaltcells-2009","author_short":["Temime-Smaali, N.","Guittat, L.","Sidibe, A.","Shin-ya, K.","Trentesaux, C.","Riou, J."],"bibdata":{"bibtype":"article","type":"article","title":"The G-quadruplex ligand telomestatin impairs binding of topoisomerase IIIalpha to G-quadruplex-forming oligonucleotides and uncaps telomeres in ALT cells.","volume":"4","issn":"1932-6203","url":"http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2732903&tool=pmcentrez&rendertype=abstract","doi":"10.1371/journal.pone.0006919","abstract":"In Alternative Lengthening of Telomeres (ALT) cell lines, specific nuclear bodies called APBs (ALT-associated PML bodies) concentrate telomeric DNA, shelterin components and recombination factors associated with telomere recombination. Topoisomerase IIIalpha (Topo III) is an essential telomeric-associated factor in ALT cells. We show here that the binding of Topo III to telomeric G-overhang is modulated by G-quadruplex formation. Topo III binding to G-quadruplex-forming oligonucleotides was strongly inhibited by telomestatin, a potent and specific G-quadruplex ligand. In ALT cells, telomestatin treatment resulted in the depletion of the Topo III/BLM/TRF2 complex and the disruption of APBs and led to the segregation of PML, shelterin components and Topo III. Interestingly, a DNA damage response was observed at telomeres in telomestatin-treated cells. These data indicate the importance of G-quadruplex stabilization during telomere maintenance in ALT cells. The function of TRF2/Topo III/BLM in the resolution of replication intermediates at telomeres is discussed.","number":"9","journal":"PloS one","author":[{"propositions":[],"lastnames":["Temime-Smaali"],"firstnames":["Nassima"],"suffixes":[]},{"propositions":[],"lastnames":["Guittat"],"firstnames":["Lionel"],"suffixes":[]},{"propositions":[],"lastnames":["Sidibe"],"firstnames":["Assitan"],"suffixes":[]},{"propositions":[],"lastnames":["Shin-ya"],"firstnames":["Kazuo"],"suffixes":[]},{"propositions":[],"lastnames":["Trentesaux"],"firstnames":["Chantal"],"suffixes":[]},{"propositions":[],"lastnames":["Riou"],"firstnames":["Jean-François"],"suffixes":[]}],"month":"January","year":"2009","pmid":"19742304","keywords":"#nosource, Biological, Cell Nucleus, Cell Nucleus: metabolism, Cell Separation, Cells, Cultured, DNA Topoisomerases, Flow Cytometry, G-Quadruplexes, Genetic, Humans, Ligands, Models, Oligonucleotides, Oligonucleotides: chemistry, Oxazoles, Oxazoles: metabolism, Protein Binding, Protein Structure, Recombination, Telomere, Telomere: metabolism, Telomere: ultrastructure, Tertiary, Type I, Type I: metabolism","pages":"e6919","bibtex":"@article{temime-smaali_g-quadruplex_2009,\n\ttitle = {The {G}-quadruplex ligand telomestatin impairs binding of topoisomerase {IIIalpha} to {G}-quadruplex-forming oligonucleotides and uncaps telomeres in {ALT} cells.},\n\tvolume = {4},\n\tissn = {1932-6203},\n\turl = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2732903&tool=pmcentrez&rendertype=abstract},\n\tdoi = {10.1371/journal.pone.0006919},\n\tabstract = {In Alternative Lengthening of Telomeres (ALT) cell lines, specific nuclear bodies called APBs (ALT-associated PML bodies) concentrate telomeric DNA, shelterin components and recombination factors associated with telomere recombination. Topoisomerase IIIalpha (Topo III) is an essential telomeric-associated factor in ALT cells. We show here that the binding of Topo III to telomeric G-overhang is modulated by G-quadruplex formation. Topo III binding to G-quadruplex-forming oligonucleotides was strongly inhibited by telomestatin, a potent and specific G-quadruplex ligand. In ALT cells, telomestatin treatment resulted in the depletion of the Topo III/BLM/TRF2 complex and the disruption of APBs and led to the segregation of PML, shelterin components and Topo III. Interestingly, a DNA damage response was observed at telomeres in telomestatin-treated cells. These data indicate the importance of G-quadruplex stabilization during telomere maintenance in ALT cells. The function of TRF2/Topo III/BLM in the resolution of replication intermediates at telomeres is discussed.},\n\tnumber = {9},\n\tjournal = {PloS one},\n\tauthor = {Temime-Smaali, Nassima and Guittat, Lionel and Sidibe, Assitan and Shin-ya, Kazuo and Trentesaux, Chantal and Riou, Jean-François},\n\tmonth = jan,\n\tyear = {2009},\n\tpmid = {19742304},\n\tkeywords = {\\#nosource, Biological, Cell Nucleus, Cell Nucleus: metabolism, Cell Separation, Cells, Cultured, DNA Topoisomerases, Flow Cytometry, G-Quadruplexes, Genetic, Humans, Ligands, Models, Oligonucleotides, Oligonucleotides: chemistry, Oxazoles, Oxazoles: metabolism, Protein Binding, Protein Structure, Recombination, Telomere, Telomere: metabolism, Telomere: ultrastructure, Tertiary, Type I, Type I: metabolism},\n\tpages = {e6919},\n}\n\n","author_short":["Temime-Smaali, N.","Guittat, L.","Sidibe, A.","Shin-ya, K.","Trentesaux, C.","Riou, J."],"key":"temime-smaali_g-quadruplex_2009","id":"temime-smaali_g-quadruplex_2009","bibbaseid":"temimesmaali-guittat-sidibe-shinya-trentesaux-riou-thegquadruplexligandtelomestatinimpairsbindingoftopoisomeraseiiialphatogquadruplexformingoligonucleotidesanduncapstelomeresinaltcells-2009","role":"author","urls":{"Paper":"http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2732903&tool=pmcentrez&rendertype=abstract"},"keyword":["#nosource","Biological","Cell Nucleus","Cell Nucleus: metabolism","Cell Separation","Cells","Cultured","DNA Topoisomerases","Flow Cytometry","G-Quadruplexes","Genetic","Humans","Ligands","Models","Oligonucleotides","Oligonucleotides: chemistry","Oxazoles","Oxazoles: metabolism","Protein Binding","Protein Structure","Recombination","Telomere","Telomere: metabolism","Telomere: ultrastructure","Tertiary","Type I","Type I: metabolism"],"metadata":{"authorlinks":{}},"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/eric.larG4","dataSources":["4i5C7S78DvJNsaHyg","5L2zM5wNE5CBYNuea"],"keywords":["#nosource","biological","cell nucleus","cell nucleus: metabolism","cell separation","cells","cultured","dna topoisomerases","flow cytometry","g-quadruplexes","genetic","humans","ligands","models","oligonucleotides","oligonucleotides: chemistry","oxazoles","oxazoles: metabolism","protein binding","protein structure","recombination","telomere","telomere: metabolism","telomere: ultrastructure","tertiary","type i","type i: metabolism"],"search_terms":["quadruplex","ligand","telomestatin","impairs","binding","topoisomerase","iiialpha","quadruplex","forming","oligonucleotides","uncaps","telomeres","alt","cells","temime-smaali","guittat","sidibe","shin-ya","trentesaux","riou"],"title":"The G-quadruplex ligand telomestatin impairs binding of topoisomerase IIIalpha to G-quadruplex-forming oligonucleotides and uncaps telomeres in ALT cells.","year":2009}