Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo

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 TEB...

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Published inNature structural & molecular biology Vol. 12; no. 10; pp. 847 - 854
Main Authors Rhodes, Daniela, Lipps, Hans Joachim, Paeschke, Katrin, Simonsson, Tomas, Postberg, Jan
Format Journal Article
LanguageEnglish
Published United States Nature Publishing Group 01.10.2005
Subjects
Animals
Binding proteins
Cell Nucleus - genetics
Cell Nucleus - metabolism
Ciliophora - genetics
Ciliophora - metabolism
Crystal structure
Deoxyribonucleic acid
DNA
DNA - chemistry
DNA - metabolism
G-Quadruplexes
Guanine - chemistry
Molecular biology
Molecular Sequence Data
Nucleic Acid Conformation
Phosphorylation
Physiological aspects
Proteins
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
RNA Interference
Structure
Telomerase
Telomere - chemistry
Telomere - metabolism
Telomere-Binding Proteins - analysis
Telomere-Binding Proteins - genetics
Telomere-Binding Proteins - metabolism
Telomeres
Yeast
Germany
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Summary: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.
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ISSN:1545-9993
1545-9985
DOI:10.1038/nsmb982