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.
Unfolding of tetraplex structure of mouse telomeric DNA by the interaction with mouse telomeric DNA binding protein Pot1. Publishing Authors By Initials
Unfolding of tetraplex structure of mouse telomeric DNA by the interaction with mouse telomeric DNA binding protein Pot1. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Nucleic acids symposium series (2004)
VOLUME:
Page Numbers: 249-50
Journal Abbreviation: Nucleic Acids Symp Ser (Oxf)
ISSN: 1746-8272
DAY: 21
MONTH: 11
YEAR: 2007
Unfolding of tetraplex structure of mouse telomeric DNA by the interaction with mouse telomeric DNA binding protein Pot1. Information
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LANGUAGE: eng
NlmUniqueID: 101259965
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Grant and Affiliation Information for Unfolding of tetraplex structure of mouse telomeric DNA by the interaction with mouse telomeric DNA binding protein Pot1.
AFFILIATION: Department of Applied Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan.
Country: England
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MEDLINETA: Nucleic Acids Symp Ser (Oxf)
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