| BRÁZDA, Václav, Jana ČECHOVÁ, M BATTISTIN, Jan COUFAL, Eva BRÁZDOVÁ JAGELSKÁ, I RAIMONDI and A INGA. The structure formed by inverted repeats in p53 response elements determines the transactivation activity of p53 protein. Biochemical and biophysical research communications. SAN DIEGO: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2017, vol. 483, No 1, p. 516-521. ISSN 0006-291X. Available from: https://dx.doi.org/10.1016/j.bbrc.2016.12.113. |
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@article{1434638,
author = {Brázda, Václav and Čechová, Jana and Battistin, M and Coufal, Jan and Brázdová Jagelská, Eva and Raimondi, I and Inga, A},
article_location = {SAN DIEGO},
article_number = {1},
doi = {http://dx.doi.org/10.1016/j.bbrc.2016.12.113},
keywords = {Inverted repeat; p53 protein; Protein-DNA interaction; Cruciform structure},
language = {eng},
issn = {0006-291X},
journal = {Biochemical and biophysical research communications},
title = {The structure formed by inverted repeats in p53 response elements determines the transactivation activity of p53 protein},
url = {http://dx.doi.org/10.1016/j.bbrc.2016.12.113},
volume = {483},
year = {2017}
}
TY - JOUR
ID - 1434638
AU - Brázda, Václav - Čechová, Jana - Battistin, M - Coufal, Jan - Brázdová Jagelská, Eva - Raimondi, I - Inga, A
PY - 2017
TI - The structure formed by inverted repeats in p53 response elements determines the transactivation activity of p53 protein
JF - Biochemical and biophysical research communications
VL - 483
IS - 1
SP - 516-521
EP - 516-521
PB - ACADEMIC PRESS INC ELSEVIER SCIENCE
SN - 0006291X
KW - Inverted repeat
KW - p53 protein
KW - Protein-DNA interaction
KW - Cruciform structure
UR - http://dx.doi.org/10.1016/j.bbrc.2016.12.113
L2 - http://dx.doi.org/10.1016/j.bbrc.2016.12.113
N2 - The TP53 gene is the most frequently mutated gene in human cancer and p53 protein plays a crucial role in gene expression and cancer protection. Its role is manifested by interactions with other proteins and DNA. p53 is a transcription factor that binds to DNA response elements (REs). Due to the palindromic nature of the consensus binding site, several p53-REs have the potential to form cruciform structures. However, the influence of cruciform formation on the activity of p53-REs has not been evaluated. Therefore, we prepared sets of p53-REs with identical theoretical binding affinity in their linear state, but different probabilities to form extra helical structures, for in vitro and in vivo analyses. Then we evaluated the presence of cruciform structures when inserted into plasmid DNA and employed a yeast-based assay to measure transactivation potential of these p53-REs cloned at a chromosomal locus in isogenic strains. We show that transactivation in vivo correlated more with relative propensity of an RE to form cruciforms than to its predicted in vitro DNA binding affinity for wild type p53. Structural features of p53-REs could therefore be an important determinant of p53 transactivation function. (C) 2016 Elsevier Inc. All rights reserved.
ER -
BRÁZDA, Václav, Jana ČECHOVÁ, M BATTISTIN, Jan COUFAL, Eva BRÁZDOVÁ JAGELSKÁ, I RAIMONDI and A INGA. The structure formed by inverted repeats in p53 response elements determines the transactivation activity of p53 protein. \textit{Biochemical and biophysical research communications}. SAN DIEGO: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2017, vol.~483, No~1, p.~516-521. ISSN~0006-291X. Available from: https://dx.doi.org/10.1016/j.bbrc.2016.12.113.
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