Highly Polymorphic G-quadruplexes in the c-MYC Promoter

Yoon, Jeongmin; Kang, Hong Je; Sung, Jaeho; Park, Hyun-Ju; Hohng, Sungchul

doi:10.5012/bkcs.2010.31.04.1025

Cited by 5 publications

(3 citation statements)

References 25 publications

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“…The binding of TMPyP4 to the wild type h c-myc GQ structure is disrupted by G to A exchange mutations which distorted the flat structure of guanine-tetrad layers [3] , [4] . The GQ structure is organized from the five guanine stretches present in the NHE III 1 region by selecting four different ones to create various isomorphic GQ structures [9] . Experiments indicate that the basket form is the thermodynamically favored form, while the kinetically favored form is the chair one [46] .…”

Section: Discussionmentioning

confidence: 99%

“…In the promoter region of the c-myc gene there are multiple nuclease hypersensitive sites. The NHE III 1 site contains guanine rich segments, which have the ability to form isomorphic GQ structures, which are in equilibrium with the double-stranded B-DNA form of that region [3] , [9] . The protruding GQ structure and the I-motif formed on the opposite strand keep the two DNA strands separated and prevent the formation of the basal transcriptional complex.…”

Section: Introductionmentioning

confidence: 99%

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The Guanine-Quadruplex Structure in the Human c-myc Gene's Promoter Is Converted into B-DNA Form by the Human Poly(ADP-Ribose)Polymerase-1

et al. 2012

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The important regulatory role of the guanine-quadruplex (GQ) structure, present in the nuclease hypersensitive element (NHE) III1 region of the human c-myc (h c-myc) gene's promoter, in the regulation of the transcription of that gene has been documented. Here we present evidences, that the human nuclear poly(ADP-ribose)polymerase-1 (h PARP-1) protein participates in the regulation of the h c-myc gene expression through its interaction with this GQ structure, characterized by binding assays, fluorescence energy transfer (FRET) experiments and by affinity pull-down experiments in vitro, and by chromatin immunoprecipitation (ChIP)-qPCR analysis and h c-myc-promoter-luciferase reporter determinations in vivo. We surmise that h PARP-1 binds to the GQ structure and participates in the conversion of that structure into the transcriptionally more active B-DNA form. The first Zn-finger structure present in h PARP-1 participates in this interaction. PARP-1 might be a new member of the group of proteins participating in the regulation of transcription through their interactions with GQ structures present in the promoters of different genes.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Guanine-Quadruplex Structure in the Human c-myc Gene's Promoter Is Converted into B-DNA Form by the Human Poly(ADP-Ribose)Polymerase-1

et al. 2012

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“…The C-rich strand in this region can form an i-motif DNA secondary structure. Single stranded G-quadruplex and i-motif structures in NHE III 1 sequence can energetically compete with the double-stranded form of DNA in this region [7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

A spectroscopic investigation of the interaction between c-MYC DNA and tetrapyridinoporphyrazinatozinc(II)

et al. 2014

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The c-MYC gene plays an important role in the regulation of cell proliferation and growth and it is overexpressed in a wide variety of human cancers. Around 90% of c-MYC transcription is controlled by the nuclease-hypersensitive element III1 (NHE III1), whose 27-nt purine-rich strand has the ability to form a G-quadruplex structure under physiological conditions. Therefore, c-MYC DNA is an attractive target for drug design, especially for cancer chemotherapy. Here, the interaction of water-soluble tetrapyridinoporphyrazinatozinc(II) with 27-nt G-rich strand (G/c-MYC), its equimolar mixture with the complementary sequence (GC/c-MYC) and related C-rich oligonucleotide (C/c-MYC) is investigated. Circular dichroism (CD) measurements of the G-rich 27-mer oligonucleotide in 150 mM KCl, pH 7 demonstrate a spectral signature consistent with parallel G-quadruplex DNA. Furthermore, the CD spectrum of the GC rich oligonucleotide shows characteristics of both duplex and quadruplex structures. Absorption spectroscopy implies that the complex binding of G/c-MYC and GC/c-MYC is a two-step process; in the first step, a very small red shift and hypochromicity and in the second step, a large red shift and hyperchromicity are observed in the Q band. Emission spectra of zinc porphyrazine are quenched upon addition of three types of DNA. According to the results of spectroscopy, it can be concluded the dominant binding mode is probably, outside binding and end stacking.

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Novel Interaction of the Z-DNA Binding Domain of Human ADAR1 with the Oncogenic c-Myc Promoter G-Quadruplex

Kang

Kim

et al. 2014

Journal of Molecular Biology

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Highly Polymorphic G-quadruplexes in the c-MYC Promoter

Cited by 5 publications

References 25 publications

The Guanine-Quadruplex Structure in the Human c-myc Gene's Promoter Is Converted into B-DNA Form by the Human Poly(ADP-Ribose)Polymerase-1

The Guanine-Quadruplex Structure in the Human c-myc Gene's Promoter Is Converted into B-DNA Form by the Human Poly(ADP-Ribose)Polymerase-1

A spectroscopic investigation of the interaction between c-MYC DNA and tetrapyridinoporphyrazinatozinc(II)

Novel Interaction of the Z-DNA Binding Domain of Human ADAR1 with the Oncogenic c-Myc Promoter G-Quadruplex

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