-
Je něco špatně v tomto záznamu ?
p53 binds human telomeric G-quadruplex in vitro
M. Adámik, I. Kejnovská, P. Bažantová, M. Petr, D. Renčiuk, M. Vorlíčková, M. Brázdová,
Jazyk angličtina Země Francie
Typ dokumentu časopisecké články
- MeSH
- cirkulární dichroismus MeSH
- DNA chemie genetika metabolismus MeSH
- draslík chemie MeSH
- ELISA MeSH
- G-kvadruplexy * MeSH
- kompetitivní vazba MeSH
- lidé MeSH
- mesoporfyriny chemie MeSH
- mutace MeSH
- nádorový supresorový protein p53 chemie genetika metabolismus MeSH
- oligonukleotidy chemie genetika metabolismus MeSH
- retardační test MeSH
- sekvence nukleotidů MeSH
- tandemové repetitivní sekvence genetika MeSH
- telomery chemie genetika metabolismus MeSH
- vazba proteinů MeSH
- vazebná místa genetika MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
The tumor suppressor protein p53 is a key factor in genome stability and one of the most studied of DNA binding proteins. This is the first study on the interaction of wild-type p53 with guanine quadruplexes formed by the human telomere sequence. Using electromobility shift assay and ELISA, we show that p53 binding to telomeric G-quadruplexes increases with the number of telomeric repeats. Further, p53 strongly favors G-quadruplexes folded in potassium over those formed in sodium, thus indicating the telomeric G-quadruplex conformational selectivity of p53. The presence of the quadruplex-stabilizing ligand, N-methyl mesoporphyrin IX (NMM), increases p53 recognition of G-quadruplexes in potassium. Using deletion mutants and selective p53 core domain oxidation, both p53 DNA binding domains are shown to be crucial for telomeric G-quadruplex recognition.
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc17013663
- 003
- CZ-PrNML
- 005
- 20170428101302.0
- 007
- ta
- 008
- 170413s2016 fr f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1016/j.biochi.2016.07.004 $2 doi
- 035 __
- $a (PubMed)27422117
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a fr
- 100 1_
- $a Adámik, Matej $u Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Kralovopolska 135, CZ-612 65 Brno, Czech Republic. $7 gn_A_00001382
- 245 10
- $a p53 binds human telomeric G-quadruplex in vitro / $c M. Adámik, I. Kejnovská, P. Bažantová, M. Petr, D. Renčiuk, M. Vorlíčková, M. Brázdová,
- 520 9_
- $a The tumor suppressor protein p53 is a key factor in genome stability and one of the most studied of DNA binding proteins. This is the first study on the interaction of wild-type p53 with guanine quadruplexes formed by the human telomere sequence. Using electromobility shift assay and ELISA, we show that p53 binding to telomeric G-quadruplexes increases with the number of telomeric repeats. Further, p53 strongly favors G-quadruplexes folded in potassium over those formed in sodium, thus indicating the telomeric G-quadruplex conformational selectivity of p53. The presence of the quadruplex-stabilizing ligand, N-methyl mesoporphyrin IX (NMM), increases p53 recognition of G-quadruplexes in potassium. Using deletion mutants and selective p53 core domain oxidation, both p53 DNA binding domains are shown to be crucial for telomeric G-quadruplex recognition.
- 650 _2
- $a sekvence nukleotidů $7 D001483
- 650 _2
- $a vazebná místa $x genetika $7 D001665
- 650 _2
- $a kompetitivní vazba $7 D001667
- 650 _2
- $a cirkulární dichroismus $7 D002942
- 650 _2
- $a DNA $x chemie $x genetika $x metabolismus $7 D004247
- 650 _2
- $a retardační test $7 D024202
- 650 _2
- $a ELISA $7 D004797
- 650 12
- $a G-kvadruplexy $7 D054856
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a mesoporfyriny $x chemie $7 D008652
- 650 _2
- $a mutace $7 D009154
- 650 _2
- $a oligonukleotidy $x chemie $x genetika $x metabolismus $7 D009841
- 650 _2
- $a draslík $x chemie $7 D011188
- 650 _2
- $a vazba proteinů $7 D011485
- 650 _2
- $a tandemové repetitivní sekvence $x genetika $7 D020080
- 650 _2
- $a telomery $x chemie $x genetika $x metabolismus $7 D016615
- 650 _2
- $a nádorový supresorový protein p53 $x chemie $x genetika $x metabolismus $7 D016159
- 655 _2
- $a časopisecké články $7 D016428
- 700 1_
- $a Kejnovská, Iva $u Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Kralovopolska 135, CZ-612 65 Brno, Czech Republic.
- 700 1_
- $a Bažantová, Pavla $u Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Kralovopolska 135, CZ-612 65 Brno, Czech Republic.
- 700 1_
- $a Petr, Marek $u Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Kralovopolska 135, CZ-612 65 Brno, Czech Republic.
- 700 1_
- $a Renčiuk, Daniel $u Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Kralovopolska 135, CZ-612 65 Brno, Czech Republic.
- 700 1_
- $a Vorlíčková, Michaela $u Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Kralovopolska 135, CZ-612 65 Brno, Czech Republic.
- 700 1_
- $a Brázdová, Marie $u Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Kralovopolska 135, CZ-612 65 Brno, Czech Republic. Electronic address: maruska@ibp.cz.
- 773 0_
- $w MED00009325 $t Biochimie $x 1638-6183 $g Roč. 128-129, č. - (2016), s. 83-91
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/27422117 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20170413 $b ABA008
- 991 __
- $a 20170428101623 $b ABA008
- 999 __
- $a ok $b bmc $g 1200128 $s 974441
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2016 $b 128-129 $c - $d 83-91 $e 20160712 $i 1638-6183 $m Biochimie $n Biochimie $x MED00009325
- LZP __
- $a Pubmed-20170413
