Unfolding of tetraplex structure of mouse telomeric DNA by the interaction with mouse telomeric DNA binding protein Pot1.
We analyzed the structural properties of mouse telomeric DNA sequence, Tel3.5: 5'-AGGG(TTAGG G)3-3', and nontelomeric DNA sequence, T22: 5'-T22-3', and examined the interaction with a single-stranded telomeric DNA-binding domain of mouse telomeric DNA-binding protein Pot1 (mPot1DBD). T22 did not form any higher-order structure, but Tel3.5 formed antiparallel tetraplex structure in the presence of Na(+). The antiparallel tetraplex of Tel3.5 became unfolded upon the interaction with mPot1DBD. Considering that the antiparallel tetraplex is known to inhibit telomerase-mediated telomere elongation, we conclude that the ability of Pot1 to unfold the antiparallel tetraplex of the telomeric DNA is required for regulation of telomerase-mediated telomere elongation.
Torigoe
Hidetaka
H
Department of Applied Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan.
Kaneda
Kaoru
K
D000818:Animals; D002942:Circular Dichroism; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D031541:Fluorescence Resonance Energy Transfer; D054856:G-Quadruplexes; D051379:Mice; D000089804:Shelterin Complex; D016615:Telomere / Q000737:chemistry*; D034501:Telomere-Binding Proteins
D004268:DNA-Binding Proteins; C507326:POT1 protein, mouse; D000089804:Shelterin Complex; D034501:Telomere-Binding Proteins; D004247:DNA