Počet záznamů: 1
p53 Binds Preferentially to Non-B DNA Structures Formed by the Pyrimidine-Rich Strands of GAA center dot TTC Trinucleotide Repeats Associated with Friedreich's Ataxia
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SYSNO ASEP 0520186 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název p53 Binds Preferentially to Non-B DNA Structures Formed by the Pyrimidine-Rich Strands of GAA center dot TTC Trinucleotide Repeats Associated with Friedreich's Ataxia Tvůrce(i) Helma, Robert (BFU-R) ORCID
Bažantová, Pavla (BFU-R)
Petr, Marek (BFU-R) ORCID
Adámik, Matěj (BFU-R) ORCID
Renčiuk, Daniel (BFU-R) RID, ORCID
Tichý, Vlastimil (BFU-R) RID
Pastuchová, Alena (BFU-R) ORCID
Soldanová, Zuzana (BFU-R) ORCID
Pečinka, Petr (BFU-R) RID
Bowater, R. P. (GB)
Fojta, Miroslav (BFU-R) RID, ORCID
Brázdová, Marie (BFU-R) RID, ORCIDCelkový počet autorů 12 Číslo článku 2078 Zdroj.dok. Molecules. - : MDPI
Roč. 24, č. 11 (2019)Poč.str. 14 s. Forma vydání Online - E Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova dynamic mutations ; disease ; length Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology CEP GA19-15168S GA ČR - Grantová agentura ČR GA16-01625S GA ČR - Grantová agentura ČR GJ17-19170Y GA ČR - Grantová agentura ČR EF15_003/0000477 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Open access Institucionální podpora BFU-R - RVO:68081707 UT WOS 000472631000051 DOI 10.3390/molecules24112078 Anotace Expansions of trinucleotide repeats (TNRs) are associated with genetic disorders such as Friedreich's ataxia. The tumor suppressor p53 is a central regulator of cell fate in response to different types of insults. Sequence and structure-selective modes of DNA recognition are among the main attributes of p53 protein. The focus of this work was analysis of the p53 structure-selective recognition of TNRs associated with human neurodegenerative diseases. Here, we studied binding of full length p53 and several deletion variants to TNRs folded into DNA hairpins or loops. We demonstrate that p53 binds to all studied non-B DNA structures, with a preference for non-B DNA structures formed by pyrimidine (Py) rich strands. Using deletion mutants, we determined the C-terminal DNA binding domain of p53 to be crucial for recognition of such non-B DNA structures. We also observed that p53 in vitro prefers binding to the Py-rich strand over the purine (Pu) rich strand in non-B DNA substrates formed by sequence derived from the first intron of the frataxin gene. The binding of p53 to this region was confirmed using chromatin immunoprecipitation in human Friedreich's ataxia fibroblast and adenocarcinoma cells. Altogether these observations provide further evidence that p53 binds to TNRs' non-B DNA structures. Pracoviště Biofyzikální ústav Kontakt Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Rok sběru 2020 Elektronická adresa https://www.mdpi.com/1420-3049/24/11/2078/pdf
Počet záznamů: 1