Redox state of p63 and p73 core domains regulates
sequence-specific DNA binding

J 2013

Redox state of p63 and p73 core domains regulates sequence-specific DNA binding

TICHÝ, Vlastimil, Lucie NAVRÁTILOVÁ, Matej ADÁMIK, Miroslav FOJTA, Marie BRÁZDOVÁ et. al.

Základní údaje

Originální název

Redox state of p63 and p73 core domains regulates sequence-specific DNA binding

Autoři

TICHÝ, Vlastimil, Lucie NAVRÁTILOVÁ, Matej ADÁMIK, Miroslav FOJTA a Marie BRÁZDOVÁ

Vydání

Biochemical and biophysical research communications, SAN DIEGO, ACADEMIC PRESS INC ELSEVIER SCIENCE, 2013, 0006-291X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

Genetika a molekulární biologie

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.281

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.bbrc.2013.02.097

UT WoS

000318259100016

Klíčová slova anglicky

p53 protein family; Tumor suppressor; Sequence-specific DNA binding; Redox state; EMSA; Zinc; Cysteine; Transcription factor; Oxidative stress

Štítky

neMU

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 17. 4. 2015 10:34, Martina Prášilová

Anotace

V originále

Cysteine oxidation and covalent modification of redox sensitive transcription factors including p53 are known, among others, as important events in cell response to oxidative stress. All p53 family proteins p53, p63 and p73 act as stress-responsive transcription factors. Oxidation of p53 central DNA binding domain destroys its structure and abolishes its sequence-specific binding by affecting zinc ion coordination at the protein-DNA interface. Proteins p63 and p73 can bind the same response elements as p53 but exhibit distinct functions. Moreover, all three proteins contain highly conserved cysteines in central DNA binding domain suitable for possible redox modulation. In this work we report for the first time the redox sensitivity of p63 and p73 core domains to a thiol oxidizing agent azodicarboxylic acid bis[dimethylamide] (diamide). Oxidation of both p63 and p73 abolished sequence-specific binding to p53 consensus sequence, depending on the agent concentration. In the presence of specific DNA all p53 family core domains were partially protected against loss of DNA binding activity due to diamide treatment. Furthermore, we detected conditional reversibility of core domain oxidation for all p53 family members and a role of zinc ions in this process. We showed that p63 and p73 proteins had greater ability to resist the diamide oxidation in comparison with p53. Our results show p63 and p73 as redox sensitive proteins with possible functionality in response of p53 family proteins to oxidative stress. (C) 2013 Elsevier Inc. All rights reserved.

Citovat

TICHÝ, Vlastimil, Lucie NAVRÁTILOVÁ, Matej ADÁMIK, Miroslav FOJTA a Marie BRÁZDOVÁ. Redox state of p63 and p73 core domains regulates sequence-specific DNA binding. Biochemical and biophysical research communications. SAN DIEGO: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2013, roč. 433, č. 4, s. 445-449. ISSN 0006-291X. Dostupné z: https://dx.doi.org/10.1016/j.bbrc.2013.02.097.

@article{1163355,
   author = {Tichý, Vlastimil and Navrátilová, Lucie and Adámik, Matej and Fojta, Miroslav and Brázdová, Marie},
   article_location = {SAN DIEGO},
   article_number = {4},
   doi = {http://dx.doi.org/10.1016/j.bbrc.2013.02.097},
   keywords = {p53 protein family; Tumor suppressor; Sequence-specific DNA binding; Redox state; EMSA; Zinc; Cysteine; Transcription factor; Oxidative stress},
   language = {eng},
   issn = {0006-291X},
   journal = {Biochemical and biophysical research communications},
   title = {Redox state of p63 and p73 core domains regulates sequence-specific DNA binding},
   volume = {433},
   year = {2013}
}

TY  - JOUR
ID  - 1163355
AU  - Tichý, Vlastimil - Navrátilová, Lucie - Adámik, Matej - Fojta, Miroslav - Brázdová, Marie
PY  - 2013
TI  - Redox state of p63 and p73 core domains regulates sequence-specific DNA binding
JF  - Biochemical and biophysical research communications
VL  - 433
IS  - 4
SP  - 445-449
EP  - 445-449
PB  - ACADEMIC PRESS INC ELSEVIER SCIENCE
SN  - 0006291X
KW  - p53 protein family
KW  - Tumor suppressor
KW  - Sequence-specific DNA binding
KW  - Redox state
KW  - EMSA
KW  - Zinc
KW  - Cysteine
KW  - Transcription factor
KW  - Oxidative stress
N2  - Cysteine oxidation and covalent modification of redox sensitive transcription factors including p53 are known, among others, as important events in cell response to oxidative stress. All p53 family proteins p53, p63 and p73 act as stress-responsive transcription factors. Oxidation of p53 central DNA binding domain destroys its structure and abolishes its sequence-specific binding by affecting zinc ion coordination at the protein-DNA interface. Proteins p63 and p73 can bind the same response elements as p53 but exhibit distinct functions. Moreover, all three proteins contain highly conserved cysteines in central DNA binding domain suitable for possible redox modulation. In this work we report for the first time the redox sensitivity of p63 and p73 core domains to a thiol oxidizing agent azodicarboxylic acid bis[dimethylamide] (diamide). Oxidation of both p63 and p73 abolished sequence-specific binding to p53 consensus sequence, depending on the agent concentration. In the presence of specific DNA all p53 family core domains were partially protected against loss of DNA binding activity due to diamide treatment. Furthermore, we detected conditional reversibility of core domain oxidation for all p53 family members and a role of zinc ions in this process. We showed that p63 and p73 proteins had greater ability to resist the diamide oxidation in comparison with p53. Our results show p63 and p73 as redox sensitive proteins with possible functionality in response of p53 family proteins to oxidative stress. (C) 2013 Elsevier Inc. All rights reserved.
ER  -

TICHÝ, Vlastimil, Lucie NAVRÁTILOVÁ, Matej ADÁMIK, Miroslav FOJTA a Marie BRÁZDOVÁ. Redox state of p63 and p73 core domains regulates sequence-specific DNA binding. \textit{Biochemical and biophysical research communications}. SAN DIEGO: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2013, roč.~433, č.~4, s.~445-449. ISSN~0006-291X. Dostupné z: https://dx.doi.org/10.1016/j.bbrc.2013.02.097.

Podrobný výpis o publikaci