The dynamic character of the G-quadruplex element in the c-MYC promoter and modification by TMPyP4

Jeyaprakashnarayanan Seenisamy; Evonne M. Rezler; Tiffanie J. Powell; Denise Tye; Vijay Gokhale; Chandana Sharma Joshi; Adam Siddiqui-Jain; Laurence H. Hurley

doi:10.1021/ja040022b

The dynamic character of the G-quadruplex element in the c-MYC promoter and modification by TMPyP4

Jeyaprakashnarayanan Seenisamy
, Evonne M. Rezler
, Tiffanie J. Powell
, Denise Tye
, Vijay Gokhale
, Chandana Sharma Joshi
, Adam Siddiqui-Jain
, Laurence H. Hurley

Research output: Contribution to journal › Article › peer-review

369 Scopus citations

Abstract

The nuclease hypersensitivity element III₁ (NHE III₁) upstream of the P1 and P2 promoters of c-MYC controls 80-90% of the transcriptional activity of this gene. The purine-rich strand in this region can form a G-quadruplex structure that is a critical part of the silencer element for this promoter. We have demonstrated that this G-quadruplex structure can form a mixture of four biologically relevant parallel-loop isomers, which upon interaction with the cationic porphyrin TMPyP4 are converted to mixed parallel/antiparallel G-quadruplex structures.

Original language	English (US)
Pages (from-to)	8702-8709
Number of pages	8
Journal	Journal of the American Chemical Society
Volume	126
Issue number	28
DOIs	https://doi.org/10.1021/ja040022b
State	Published - Jul 21 2004

ASJC Scopus subject areas

Catalysis
Biochemistry
General Chemistry
Colloid and Surface Chemistry

Access to Document

10.1021/ja040022b

Cite this

@article{967eba832b02420d8830e72516e99291,

title = "The dynamic character of the G-quadruplex element in the c-MYC promoter and modification by TMPyP4",

abstract = "The nuclease hypersensitivity element III1 (NHE III1) upstream of the P1 and P2 promoters of c-MYC controls 80-90\% of the transcriptional activity of this gene. The purine-rich strand in this region can form a G-quadruplex structure that is a critical part of the silencer element for this promoter. We have demonstrated that this G-quadruplex structure can form a mixture of four biologically relevant parallel-loop isomers, which upon interaction with the cationic porphyrin TMPyP4 are converted to mixed parallel/antiparallel G-quadruplex structures.",

author = "Jeyaprakashnarayanan Seenisamy and Rezler, \{Evonne M.\} and Powell, \{Tiffanie J.\} and Denise Tye and Vijay Gokhale and Joshi, \{Chandana Sharma\} and Adam Siddiqui-Jain and Hurley, \{Laurence H.\}",

year = "2004",

month = jul,

day = "21",

doi = "10.1021/ja040022b",

language = "English (US)",

volume = "126",

pages = "8702--8709",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "28",

}

TY - JOUR

T1 - The dynamic character of the G-quadruplex element in the c-MYC promoter and modification by TMPyP4

AU - Seenisamy, Jeyaprakashnarayanan

AU - Rezler, Evonne M.

AU - Powell, Tiffanie J.

AU - Tye, Denise

AU - Gokhale, Vijay

AU - Joshi, Chandana Sharma

AU - Siddiqui-Jain, Adam

AU - Hurley, Laurence H.

PY - 2004/7/21

Y1 - 2004/7/21

N2 - The nuclease hypersensitivity element III1 (NHE III1) upstream of the P1 and P2 promoters of c-MYC controls 80-90% of the transcriptional activity of this gene. The purine-rich strand in this region can form a G-quadruplex structure that is a critical part of the silencer element for this promoter. We have demonstrated that this G-quadruplex structure can form a mixture of four biologically relevant parallel-loop isomers, which upon interaction with the cationic porphyrin TMPyP4 are converted to mixed parallel/antiparallel G-quadruplex structures.

AB - The nuclease hypersensitivity element III1 (NHE III1) upstream of the P1 and P2 promoters of c-MYC controls 80-90% of the transcriptional activity of this gene. The purine-rich strand in this region can form a G-quadruplex structure that is a critical part of the silencer element for this promoter. We have demonstrated that this G-quadruplex structure can form a mixture of four biologically relevant parallel-loop isomers, which upon interaction with the cationic porphyrin TMPyP4 are converted to mixed parallel/antiparallel G-quadruplex structures.

UR - https://www.scopus.com/pages/publications/3242691283

UR - https://www.scopus.com/pages/publications/3242691283#tab=citedBy

U2 - 10.1021/ja040022b

DO - 10.1021/ja040022b

M3 - Article

C2 - 15250722

AN - SCOPUS:3242691283

SN - 0002-7863

VL - 126

SP - 8702

EP - 8709

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 28

ER -

The dynamic character of the G-quadruplex element in the c-MYC promoter and modification by TMPyP4

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this