Literature DB >> 21028832

Folding equilibrium constants of telomere G-quadruplexes in free state or associated with proteins determined by isothermal differential hybridization.

Quan Wang1, Li Ma, Yu-Hua Hao, Zheng Tan.   

Abstract

Guanine rich (G-rich) nucleic acids form G-quadruplex structures that are implicated in many biological processes, pharmaceutical applications, and molecular machinery. The folding equilibrium constant (K(F)) of the G-quadruplex not only determines its stability and competition against duplex formation in genomic DNA but also defines its recognition by proteins and drugs and technical specifications. The K(F) is most conveniently derived from thermal melting analysis that has so far yielded extremely diversified results for the human telomere G-quadruplex. Melting analysis cannot be used for nucleic acids associated with proteins, thus has difficulty to study how protein association affects the folding equilibrium of G-quadruplex structure. In this work, we established an isothermal differential hybridization (IDH) method that is able to determine the K(F) of G-quadruplex, either alone or associated with proteins. Using this method, we studied the folding equilibrium of the core sequence G(3)(T(2)AG(3))(3) from vertebrate telomere in K(+) and Na(+) solutions and how it is affected by proteins associated at its adjacent regions. Our results show that the K(F) obtained for the free G-quadruplex is within 1 order of magnitude of most of those obtained by melting analysis and protein binding beside a G-quadruplex can dramatically destabilize the G-quadruplex.

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Year:  2010        PMID: 21028832     DOI: 10.1021/ac102168m

Source DB:  PubMed          Journal:  Anal Chem        ISSN: 0003-2700            Impact factor:   6.986


  5 in total

1.  Single molecule studies of physiologically relevant telomeric tails reveal POT1 mechanism for promoting G-quadruplex unfolding.

Authors:  Hong Wang; Gerald J Nora; Harshad Ghodke; Patricia L Opresko
Journal:  J Biol Chem       Date:  2010-12-23       Impact factor: 5.157

2.  Long repeating (TTAGGG) n single-stranded DNA self-condenses into compact beaded filaments stabilized by G-quadruplex formation.

Authors:  Anirban Kar; Nathan Jones; N Özlem Arat; Richard Fishel; Jack D Griffith
Journal:  J Biol Chem       Date:  2018-04-19       Impact factor: 5.157

3.  G-quadruplex formation at the 3' end of telomere DNA inhibits its extension by telomerase, polymerase and unwinding by helicase.

Authors:  Quan Wang; Jia-quan Liu; Zhao Chen; Ke-wei Zheng; Chang-yue Chen; Yu-Hua Hao; Zheng Tan
Journal:  Nucleic Acids Res       Date:  2011-03-25       Impact factor: 16.971

4.  G-quadruplex formation in telomeres enhances POT1/TPP1 protection against RPA binding.

Authors:  Sujay Ray; Jigar N Bandaria; Mohammad H Qureshi; Ahmet Yildiz; Hamza Balci
Journal:  Proc Natl Acad Sci U S A       Date:  2014-02-10       Impact factor: 12.779

5.  RecQ-core of BLM unfolds telomeric G-quadruplex in the absence of ATP.

Authors:  Jagat B Budhathoki; Sujay Ray; Vaclav Urban; Pavel Janscak; Jaya G Yodh; Hamza Balci
Journal:  Nucleic Acids Res       Date:  2014-09-22       Impact factor: 16.971

  5 in total

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