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G Lancelot

Publications and source records attributed to G Lancelot.

38 records · Page 3Linked to original sources

Selective recognition of nucleic acids by proteins: the specificity of guanine interaction with carboxylate ions.

The interaction of carboxylate ions (acetate, butyrate) with nucleic aicd bases and nucleosides has been investigated by proton magnetic resonance in dimethyl sulfoxide (d6)/H2O mixtures. Carboxylate ions interacted only with guanine derivatives and led to a large downfield shift of the NH2 resonance. A 1:1 stoichiometry was deduced from a study of the concentration dependence of chemical shifts. A study of substituted guanine showed that hydrogen bonding involved N(1)H and NH2(2). An association constant of 110 M-1 was determined. This value is about 30 times higher than the association constant for guanine-cytosine base pair formation under the same experimental conditions. As a matter of fact, carboxylate ions induced a dissociation of guanine-cytosine base pairs. This guanine-carboxylate association is experimental evidence for a highly specific interaction that could play an important role in protein/nucleic acid recognition.

Acetates↗

Oligodeoxynucleotides covalently linked to intercalating agents: a new class of gene regulatory substances.

Oligodeoxynucleotides have been covalently linked to a 9-aminoacridine derivative via their 3'-phosphate group. Specific complexes are formed with the complementary sequence of the oligonucleotide. The stability is strongly increased due to intercalation of the acridine derivative. Absorption, fluorescence, nuclear magnetic resonance and circular dichroism have been used to characterize complex formation. The stability of the complexes depends on the length of the linker between the acridine derivative and the 3'-phosphate group of the oligonucleotide. Oligonucleotides covalently linked to an intercalating agent can be used to selectively control gene expression. Transcription initiation can be blocked when such an oligonucleotide binds to the transcribed strand in the open complex formed by E. coli RNA polymerase with the bla promoter. With some oligonucleotides, non-specific effects on transcription can be detected, most probably due to binding of the modified oligonucleotide to RNA polymerase. Translation of the messenger RNA from gene 32 of phage T4 can be prevented by using an oligonucleotide complementary to the sequence upstream from the Shine-Dalgarno sequence. Inhibition of translation does not occur in the absence of the intercalating agent covalently linked to the oligonucleotide nor with oligonucleotides which do not have a target sequence on the mRNA.

DNA-Directed RNA Polymerases↗