Structure-activity relationships in polymorphic G-quadruplex
forming segment of c-MYC promoter

a 2017

Structure-activity relationships in polymorphic G-quadruplex forming segment of c-MYC promoter

RYNEŠ, Jan, T. FESSL, Michaela KRAFČÍKOVÁ, Lukáš TRANTÍREK, Silvie TRANTÍRKOVÁ et. al.

Základní údaje

Originální název

Structure-activity relationships in polymorphic G-quadruplex forming segment of c-MYC promoter

Autoři

RYNEŠ, Jan (203 Česká republika, domácí), T. FESSL (203 Česká republika), Michaela KRAFČÍKOVÁ (703 Slovensko, domácí), Lukáš TRANTÍREK (203 Česká republika, garant, domácí) a Silvie TRANTÍRKOVÁ (203 Česká republika, domácí)

Vydání

42nd Congress of the Federation-of-European-Biochemical-Societies (FEBS) on From Molecules to Cells and Back, 2017

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10608 Biochemistry and molecular biology

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.530

Kód RIV

RIV/00216224:14740/17:00095589

Organizační jednotka

Středoevropský technologický institut

ISSN

UT WoS

000409918903226

Klíčová slova anglicky

polymorphic G-quadruplex; c-MYC promoter

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 19. 3. 2018 16:51, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

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

Návaznosti

GA17-12075S, projekt VaV

Název: Polymorfní G-quadruplexy v promotorových oblastech genů

Investor: Grantová agentura ČR, Polymorfní G-quadruplexy v promotorových oblastech genů

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

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 42nd Congress of the Federation-of-European-Biochemical-Societies (FEBS) on From Molecules to Cells and Back. 2017. ISSN 1742-464X.

@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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