Počet záznamů: 1
Recognition of Local DNA Structures by p53 Protein
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SYSNO ASEP 0485741 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Recognition of Local DNA Structures by p53 Protein Tvůrce(i) Brázda, Václav (BFU-R) RID, ORCID
Coufal, Jan (BFU-R) ORCIDCelkový počet autorů 2 Číslo článku 375 Zdroj.dok. International Journal of Molecular Sciences. - : MDPI - ISSN 1661-6596
Roč. 18, č. 2 (2017)Poč.str. 5 s. Forma vydání Online - E Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova tumor-suppressor protein ; c-terminal domain ; non-b dna Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology CEP GA15-21855S GA ČR - Grantová agentura ČR Institucionální podpora BFU-R - RVO:68081707 UT WOS 000395457700143 DOI https://doi.org/10.3390/ijms18020375 Anotace p53 plays critical roles in regulating cell cycle, apoptosis, senescence and metabolism and is commonly mutated in human cancer. These roles are achieved by interaction with other proteins, but particularly by interaction with DNA. As a transcription factor, p53 is well known to bind consensus target sequences in linear B-DNA. Recent findings indicate that p53 binds with higher affinity to target sequences that form cruciform DNA structure. Moreover, p53 binds very tightly to non-B DNA structures and local DNA structures are increasingly recognized to influence the activity of wild-type and mutant p53. Apart from cruciform structures, p53 binds to quadruplex DNA, triplex DNA, DNA loops, bulged DNA and hemicatenane DNA. In this review, we describe local DNA structures and summarize information about interactions of p53 with these structural DNA motifs. These recent data provide important insights into the complexity of the p53 pathway and the functional consequences of wild-type and mutant p53 activation in normal and tumor cells. Pracoviště Biofyzikální ústav Kontakt Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Rok sběru 2018
Počet záznamů: 1