Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo. Paeschke, K., Simonsson, T., Postberg, J., Rhodes, D., & Lipps, H. J. Nature structural & molecular biology, 12(10):847–54, October, 2005. tex.ids= paeschkeTelomereEndbindingProteins2005
Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo. [link]Paper  doi  abstract   bibtex   
Telomere end-binding proteins (TEBPs) bind to the guanine-rich overhang (G-overhang) of telomeres. Although the DNA binding properties of TEBPs have been investigated in vitro, little is known about their functions in vivo. Here we use RNA interference to explore in vivo functions of two ciliate TEBPs, TEBPalpha and TEBPbeta. Silencing the expression of genes encoding both TEBPs shows that they cooperate to control the formation of an antiparallel guanine quadruplex (G-quadruplex) DNA structure at telomeres in vivo. This function seems to depend on the role of TEBPalpha in attaching telomeres in the nucleus and in recruiting TEBPbeta to these sites. In vitro DNA binding and footprinting studies confirm the in vivo observations and highlight the role of the C terminus of TEBPbeta in G-quadruplex formation. We have also found that G-quadruplex formation in vivo is regulated by the cell cycle-dependent phosphorylation of TEBPbeta.
@article{Paeschke2005,
	title = {Telomere end-binding proteins control the formation of {G}-quadruplex {DNA} structures in vivo.},
	volume = {12},
	issn = {1545-9993},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/16142245},
	doi = {10.1038/nsmb982},
	abstract = {Telomere end-binding proteins (TEBPs) bind to the guanine-rich overhang (G-overhang) of telomeres. Although the DNA binding properties of TEBPs have been investigated in vitro, little is known about their functions in vivo. Here we use RNA interference to explore in vivo functions of two ciliate TEBPs, TEBPalpha and TEBPbeta. Silencing the expression of genes encoding both TEBPs shows that they cooperate to control the formation of an antiparallel guanine quadruplex (G-quadruplex) DNA structure at telomeres in vivo. This function seems to depend on the role of TEBPalpha in attaching telomeres in the nucleus and in recruiting TEBPbeta to these sites. In vitro DNA binding and footprinting studies confirm the in vivo observations and highlight the role of the C terminus of TEBPbeta in G-quadruplex formation. We have also found that G-quadruplex formation in vivo is regulated by the cell cycle-dependent phosphorylation of TEBPbeta.},
	number = {10},
	journal = {Nature structural \& molecular biology},
	author = {Paeschke, Katrin and Simonsson, Tomas and Postberg, Jan and Rhodes, Daniela and Lipps, Hans Joachim},
	month = oct,
	year = {2005},
	pmid = {16142245},
	note = {tex.ids= paeschkeTelomereEndbindingProteins2005},
	keywords = {\#nosource, Animals, Cell Nucleus, Cell Nucleus: genetics, Cell Nucleus: metabolism, Ciliophora, Ciliophora: genetics, Ciliophora: metabolism, DNA, DNA: chemistry, DNA: metabolism, G-Quadruplexes, Guanine, Guanine: chemistry, Molecular Sequence Data, Nucleic Acid Conformation, Protozoan Proteins, Protozoan Proteins: genetics, Protozoan Proteins: metabolism, RNA Interference, Telomere, Telomere-Binding Proteins, Telomere-Binding Proteins: analysis, Telomere-Binding Proteins: genetics, Telomere-Binding Proteins: metabolism, Telomere: chemistry, Telomere: metabolism},
	pages = {847--54},
}

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