J 2018

p73, like its p53 homolog, shows preference for inverted repeats forming cruciforms

ČECHOVÁ, Jana, Jan COUFAL, Eva BRÁZDOVÁ JAGELSKÁ, Miroslav FOJTA, Václav BRÁZDA et. al.

Základní údaje

Originální název

p73, like its p53 homolog, shows preference for inverted repeats forming cruciforms

Autoři

ČECHOVÁ, Jana (203 Česká republika, domácí), Jan COUFAL (203 Česká republika), Eva BRÁZDOVÁ JAGELSKÁ (203 Česká republika), Miroslav FOJTA (203 Česká republika) a Václav BRÁZDA (203 Česká republika, garant)

Vydání

Plos one, San Francisco, Public Library of Science, 2018, 1932-6203

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Impakt faktor

Impact factor: 2.776

Kód RIV

RIV/00216224:14310/18:00108863

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000430290200060

Klíčová slova anglicky

SEQUENCE-SPECIFIC BINDING; DNA-BINDING; TRANSCRIPTIONAL ACTIVITY; SUPERCOILED DNA; BREAST-CANCER; MUTANT P53; TRANSACTIVATION; P63; PROTEIN; APOPTOSIS

Štítky

Příznaky

Recenzováno
Změněno: 11. 5. 2020 09:44, Mgr. Marie Šípková, DiS.

Anotace

V originále

p73 is a member of the p53 protein family and has essential functions in several signaling pathways involved in development, differentiation, DNA damage responses and cancer. As a transcription factor, p73 achieves these functions by binding to consensus DNA sequences and p73 shares at least partial target DNA binding sequence specificity with p53. Transcriptional activation by p73 has been demonstrated for more than fifty p53 targets in yeast and/or human cancer cell lines. It has also been shown previously that p53 binding to DNA is strongly dependent on DNA topology and the presence of inverted repeats that can form DNA cruciforms, but whether p73 transcriptional activity has similar dependence has not been investigated. Therefore, we evaluated p73 binding to a set of p53-response elements with identical theoretical binding affinity in their linear state, but different probabilities to form extra helical structures. We show by a yeast-based assay that transactivation in vivo correlated more with the relative propensity of a response element to form cruciforms than to its expected in vitro DNA binding affinity. Structural features of p73 target sites are therefore likely to be an important determinant of its transactivation function.