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@proceedings{1411820,
author = {Ryneš, Jan and Fessl, T. and Krafčíková, Michaela and Trantírek, Lukáš and Trantírková, Silvie},
booktitle = {42nd Congress of the Federation-of-European-Biochemical-Societies (FEBS) on From Molecules to Cells and Back},
keywords = {polymorphic G-quadruplex; c-MYC promoter},
language = {eng},
title = {Structure-activity relationships in polymorphic G-quadruplex forming segment of c-MYC promoter},
url = {https://2017.febscongress.org/abstract_preview.aspx?idAbstractEnc=4424170093096095099093424170},
year = {2017}
}
TY - CONF
ID - 1411820
AU - Ryneš, Jan - Fessl, T. - Krafčíková, Michaela - Trantírek, Lukáš - Trantírková, Silvie
PY - 2017
TI - Structure-activity relationships in polymorphic G-quadruplex forming segment of c-MYC promoter
KW - polymorphic G-quadruplex
KW - c-MYC promoter
UR - https://2017.febscongress.org/abstract_preview.aspx?idAbstractEnc=4424170093096095099093424170
N2 - One of the driving forces of malignant transformation is activation of a protooncogene that is converted into oncogene by a mutation, which changes the protein function or expression. Misregulation of the proto-oncogene c-Myc has been identified in many human cancers. Therefore, the detailed knowledge of c-Myc regulation is necessary to develop appropriate therapies. Expression of c-Myc is co-regulated by a G-quadruplex that can be formed from a G-rich motif Pu27 within the c-Myc promoter. Pu27 consists of five G-tracts separated by one A or T nucleotide. Formation of a Gquadruplex requires only four G-tracts. Hence, the Pu27 segment give rise to several distinct G-quadruplex conformations. It is not known, which particular G-quadruplex conformation bears the biological role. To address this point, we have prepared a set of Pu27 oligonucleotides with naturally occurring nucleotide substitutions in different G-tracts that limit the number of possible G-quadruplex conformations. Using single particle FRET, we have identified populations of the G-quadruplex topologies that the Pu27 variants form in vitro. By performing pull-downs from nuclear lysates, we have revealed proteins that bind to the particular Gquadruplexes. To test the function, Pu27 element in the human c-Myc promoter has been mutated and the activity examined in a luciferase reporter assay. Preliminary data from our experiments indicate that there are several structural topologies of Gquadruplex formed from Pu27 sequence, which are functionally equivalent
ER -
RYNEŠ, Jan, T. FESSL, Michaela KRAFČÍKOVÁ, Lukáš TRANTÍREK a Silvie TRANTÍRKOVÁ. Structure-activity relationships in polymorphic G-quadruplex forming segment of c-MYC promoter. In \textit{42nd Congress of the Federation-of-European-Biochemical-Societies (FEBS) on From Molecules to Cells and Back}. 2017. ISSN~1742-464X.
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