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Characterization of p53 Family Homologs in Evolutionary Remote Branches of Holozoa
M. Bartas, V. Brázda, J. Červeň, P. Pečinka,
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články
Grantová podpora
project LO1208 TEWEP
Ministry of Education, Youth and Sports of the Czech Republic in the "National Feasibility Program I"
18-15548S
The Czech Science Foundation
CZ.1.05/2.1.00/19.0388
EU structural funding Operational Programme Research and Development for innovation
SGS/09/PrF/2019
University of Ostrava
NLK
Directory of Open Access Journals
od 2000
Free Medical Journals
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Freely Accessible Science Journals
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PubMed Central
od 2007
Europe PubMed Central
od 2007
ProQuest Central
od 2000-03-01
Open Access Digital Library
od 2000-01-01
Open Access Digital Library
od 2007-01-01
Health & Medicine (ProQuest)
od 2000-03-01
ROAD: Directory of Open Access Scholarly Resources
od 2000
PubMed
31861340
DOI
10.3390/ijms21010006
Knihovny.cz E-zdroje
- MeSH
- databáze genetické MeSH
- Eukaryota klasifikace genetika MeSH
- exony MeSH
- fylogeneze MeSH
- interakční proteinové domény a motivy MeSH
- introny MeSH
- konformace proteinů MeSH
- molekulární evoluce * MeSH
- molekulární modely MeSH
- multigenová rodina * MeSH
- nádorový supresorový protein p53 chemie genetika metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvenční homologie aminokyselin * MeSH
- Publikační typ
- časopisecké články MeSH
The p53 family of transcription factors plays key roles in development, genome stability, senescence and tumor development, and p53 is the most important tumor suppressor protein in humans. Although intensively investigated for many years, its initial evolutionary history is not yet fully elucidated. Using bioinformatic and structure prediction methods on current databases containing newly-sequenced genomes and transcriptomes, we present a detailed characterization of p53 family homologs in remote members of the Holozoa group, in the unicellular clades Filasterea, Ichthyosporea and Corallochytrea. Moreover, we show that these newly characterized homologous sequences contain domains that can form structures with high similarity to the human p53 family DNA-binding domain, and some also show similarities to the oligomerization and SAM domains. The presence of these remote homologs demonstrates an ancient origin of the p53 protein family.
Department of Biology and Ecology University of Ostrava 710 00 Ostrava Czech Republic
Institute of Biophysics of the Czech Academy of Sciences 612 65 Brno Czech Republic
Citace poskytuje Crossref.org
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