Preferential Binding of Hot Spot Mutant p53 Proteins to Supercoiled DNA In Vitro and in Cells

Brázdová, Marie; Navrátilová, Lucie; Tichý, Vlastimil; Němcová, Kateřina; Lexa, M.; Hrstka, R.; Pečinka, Petr; Adámik, Matěj; Vojtěšek, B.; Paleček, Emil; Deppert, W.; Fojta, Miroslav

doi:https://dx.doi.org/10.1371/journal.pone.0059567

Number of the records: 1

Preferential Binding of Hot Spot Mutant p53 Proteins to Supercoiled DNA In Vitro and in Cells

1.

SYSNO ASEP	0392686
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Preferential Binding of Hot Spot Mutant p53 Proteins to Supercoiled DNA In Vitro and in Cells
Author(s)	Brázdová, Marie (BFU-R)_{RID, ORCID} Navrátilová, Lucie (BFU-R) Tichý, Vlastimil (BFU-R)_RID Němcová, Kateřina (BFU-R) Lexa, M. (CZ) Hrstka, R. (CZ) Pečinka, Petr (BFU-R)_RID Adámik, Matěj (BFU-R)_ORCID Vojtěšek, B. (CZ) Paleček, Emil (BFU-R)_{RID, ORCID} Deppert, W. (DE) Fojta, Miroslav (BFU-R)_{RID, ORCID}
Number of authors	12
Source Title	PLoS ONE. - : Public Library of Science - ISSN 1932-6203 Roč. 8, č. 3 (2013), e59567
Number of pages	17 s.
Publication form	Online - E
Language	eng - English
Country	US - United States
Keywords	TUMOR-SUPPRESSOR P53 ; C-TERMINAL DOMAIN ; OF-FUNCTION MUTATIONS
Subject RIV	BO - Biophysics
R&D Projects	GAP301/10/2370 GA ČR - Czech Science Foundation (CSF)
	GA13-36108S GA ČR - Czech Science Foundation (CSF)
	GP204/06/P369 GA ČR - Czech Science Foundation (CSF)
	GA204/08/1560 GA ČR - Czech Science Foundation (CSF)
	GAP301/11/2055 GA ČR - Czech Science Foundation (CSF)
	1K04119 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
CEZ	AV0Z50040702 - BFU-R (2007-2013)
UT WOS	000317418500055
DOI	10.1371/journal.pone.0059567
Annotation	Hot spot mutant p53 (mutp53) proteins exert oncogenic gain-of-function activities. Binding of mutp53 to DNA is assumed to be involved in mutp53-mediated repression or activation of several mutp53 target genes. To investigate the importance of DNA topology on mutp53-DNA recognition in vitro and in cells, we analyzed the interaction of seven hot spot mutp53 proteins with topologically different DNA substrates (supercoiled, linear and relaxed) containing and/or lacking mutp53 binding sites (mutp53BS) using a variety of electrophoresis and immunoprecipitation based techniques. All seven hot spot mutp53 proteins (R175H, G245S, R248W, R249S, R273C, R273H and R282W) were found to have retained the ability of wildtype p53 to preferentially bind circular DNA at native negative superhelix density, while linear or relaxed circular DNA was a poor substrate.
Workplace	Institute of Biophysics
Contact	Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244
Year of Publishing	2014

Number of the records: 1