title: p53-catalyzed annealing of complementary single-stranded nucleic acids.
abstract: p53 has been reported to inhibit the DNA helicase intrinsic to simian virus 40 large tumor antigen (T antigen). We found that inhibition is not restricted to T antigen, but also affects several other DNA and RNA helicases. Complexing of the helicases by the p53 protein as a possible inactivation mechanism could be excluded. Instead, the anti-helicase activity can be explained by our finding that p53 binds with high affinity to single-stranded nucleic acids and has a strong DNA.DNA and RNA.RNA annealing activity. We could also show that p53 is able to alter the secondary structure of RNA and/or to influence dynamic RNA-RNA interactions. These results, and the fact that the affinity of p53 to RNA is about one order of magnitude higher than to single-stranded DNA, imply an RNA-specific function of p53 in vivo.
authors.affiliation: Fakultät für Biologie, Universität Konstanz, Germany.
authors.forename: P
authors.initials: P
authors.lastname: Oberosler
authors.forename: P
authors.initials: P
authors.lastname: Hloch
authors.forename: U
authors.initials: U
authors.lastname: Ramsperger
authors.forename: H
authors.initials: H
authors.lastname: Stahl
mesh_terms: D000818:Animals; D016367:Baculoviridae; D001665:Binding Sites; D002478:Cells, Cultured; D003001:Cloning, Molecular; D004265:DNA Helicases / Q000037:antagonists & inhibitors; D004277:DNA, Single-Stranded / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008854:Microscopy, Electron; D009036:Moths; D009690:Nucleic Acid Conformation; D012313:RNA / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D020365:RNA Helicases; D012316:RNA Nucleotidyltransferases / Q000037:antagonists & inhibitors; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D004277:DNA, Single-Stranded; D016159:Tumor Suppressor Protein p53; D012313:RNA; D012316:RNA Nucleotidyltransferases; D004265:DNA Helicases; D020365:RNA Helicases