Article abstract
Nature Structural & Molecular Biology 15, 598 - 604 (2008)
Published online: 18 May 2008 | doi:10.1038/nsmb.1422
Telomerase recruitment by the telomere end binding protein-
facilitates G-quadruplex DNA unfolding in ciliates
Katrin Paeschke1, Stefan Juranek1, Tomas Simonsson2, Anne Hempel3, Daniela Rhodes3 & Hans Joachim Lipps1
Abstract
The telomeric G-overhangs of the ciliate Stylonychia lemnae fold into a G-quadruplex DNA structure in vivo. Telomeric G-quadruplex formation requires the presence of two telomere end binding proteins, TEBP
and TEBP
, and is regulated in a cell-cycle dependent manner. Unfolding of this structure in S phase is dependent on the phosphorylation of TEBP. Here we show that TEBP phosphorylation is necessary but not sufficient for a G-quadruplex unfolding rate compatible with telomere synthesis. The telomerase seems to be actively involved in telomeric G-quadruplex DNA structure unfolding in vivo. Significantly, the telomerase is recruited to telomeres by phosphorylated TEBP, and hence telomerase recruitment is cell-cycle regulated through phosphorylation. These observations allow us to propose a model for the regulation of G-quadruplex unfolding and telomere synthesis during the cell cycle.
- Institute of Cell Biology, University Witten/Herdecke, Stockumer Strasse 10, 58453 Witten, Germany.
- Institute of Biomedicine, Göteborg University, P.O. Box 440, 405 30 Göteborg, Sweden.
- Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Correspondence to: Hans Joachim Lipps1 e-mail: lipps@uni-wh.de
Correspondence to: Daniela Rhodes3 e-mail: rhodes@mrc-lmb.cam.ac.uk
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