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Nucleic Acids Research, 1990, Vol. 18, No. 19 5775-5780
© 1990

MOLECULAR BIOLOGY

The specific binding of nuclear protein(s) to the cAMP responsive element (CRE) sequence (TGACGTCA) is reduced by the misincorporation of U and increased by the deamination of C

Annalisa Verri, Paolo Mazzarello, Giuseppe Biamonti, Silvio Spadari* and Federico Focher

Istituto di Genetica Biochimica ed Evoluzionistica CNR, Via Abbiategrasso 207, 1-27100 Pavia, Italy

*To whom correspondence should be addressed

Received June 11, 1990. Revised May 5, 1990. Accepted May 5, 1990.

Point mutations In the cAMP-responsive element (CRE) of the rat somatostatin gene promoter/enhancer sequence (TGACGTCA) were used as a model for assessing the effect of uracil, deriving either from misincorporation during DNA synthesis (T->U) or cytosine deamination (C->U), on the binding of sequence/specific regulatory proteins. The results show that the T->U conversion In both strands of the CRE palindromic sequence reduces its affinity for the CRE binding factors), suggesting the crucial role of the methyl group contributed by T for the correct recognition of the sequence. On the other hand, deamination of C in the CpG central dinucleotide (CpG-UpG) causes an increase of binding affinity which is further enhanced by the contemporary deamination in both strands. Then, both uracil misincorporation and cytosine deamination alter the binding to CRE sequence In vitro, suggesting that uracil, if not removed by uracil DNA-glycosylase, could be dangerous for cellular functions.


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