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p53-catalyzed annealing of complementary single-stranded nucleic acids

Oberosler, P.; Hloch, P.; Ramsperger, U.; Stahl, H.

EMBO Journal 12(6): 2389-2396

1993

ISSN/ISBN: 0261-4189
PMID: 7685274
Document Number: 407985
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 cntdot DNA and RNA cntdot 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 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.

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