Interaction of Disulfide Groups With Nucleic Acid Bases

Montenay-Garestier, Thérèse; Brun, Francine; Hélène, Claude

doi:10.1111/j.1751-1097.1976.tb06778.x

Cited by 14 publications

(7 citation statements)

References 24 publications

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“…results seem to exclude stacking interaction in headpiece-lac operator complexes (Nick et al, 1982). For energy transfer from tyrosine to the nucleic acid bases the critical Forster distance can be as high as 20 A (Montenay-Garestier, 1975). Therefore, tyrosine fluorescence can be quenched even if the residue is not engaged in any close contact interaction (such as hydrogen bonding) with the DNA.…”

Section: Discussionmentioning

confidence: 99%

Interaction between the lac operator and the lac repressor headpiece: fluorescence and circular dichroism studies.

Culard¹,

Schnarr²,

Maurizot³

1982

The EMBO Journal

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The interaction between the lac repressor headpiece and a small operator DNA fragment has been examined by fluorescence and circular dichroism (c.d.) measurements. Binding of the headpiece to the DNA fragment induces a strong quenching of the fluorescence of its tyrosine residues. Quantitative analysis of the fluorescence data demonstrates that, in a first step, two headpieces bind very strongly to the DNA fragment then weaker binding occurs. C.d. demonstrates that the binding induces conformational changes of the DNA. The c.d. change produced upon binding of the first two headpieces differs from that induced upon binding of two further headpieces . Binding of the second pair of headpieces is similar to non‐specific binding to non‐operator DNA. The conformation of the operator DNA in the presence of two headpieces differs drastically from that in presence of lac repressor. Addition of the core to the lac operator does not induce any conformational change of the nucleic acids. These results are discussed with respect to the relative roles of core and headpieces in the lac repressor‐lac operator interaction.

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Section: Discussionmentioning

confidence: 99%

Interaction between the lac operator and the lac repressor headpiece: fluorescence and circular dichroism studies.

Culard¹,

Schnarr²,

Maurizot³

1982

The EMBO Journal

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“…Shafferman and Stein (1974) have shown that the reaction of dithioglycolic acid, an analog of cystine, to form thioglycolic acid can be photosensitized by tyrosine at acid pH through electronic energy transfer. Montenay-Garestier et al (1976) have shown that excited poly A interacts with cystamine, possibly leading to S-S bond rupture. It is possible that energy transfer or other interactions of photoexcited bases with cystine could lead to the formation of cysteine.…”

Section: Photoreactions Of Nucleic Acids and Their Constituents With mentioning

confidence: 98%

Cross-Linking of Proteins to Nucleic Acids by Ultraviolet Light

Shetlar

1980

Photochemical and Photobiological Reviews

100

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“…Energy transfer from tyrosine to nucleic acid bases appears as the most likely explanation for quenching. The calculated Forster distances for singlet energy transfer gave values ranging from 10 to 17A depending on the nature of the base (Montenay-Garestier, 1975). As methylation of the hydroxyl group does not change greatly either the overlap integrals or Forster critical distances energy transfer can explain the results obtained with peptides containing either methylated or unmethylated tyrosine residues.…”

Section: Resultsmentioning

confidence: 86%

“…Several mechanisms could explain such a quenching : (i) stacking between nucleic bases and phenol rings. This interaction was demonstrated in single stranded polynucleotide-oligopeptide complexes (Dimicoli and Helene, 1972); (ii) energy transfer from tyrosine to nucleic acid bases (Montenay-Garestier, 1975); (iii) hydrogen bonding between the hydroxyl group of tyrosine and acceptor sites of nucleic acids (Sellini et a!., 1973;Lancelot, 1977) followed by proton transfer in the excited state; (iv) a protein conformational change which brings an inhibitor group of the peptidic chain in the vicinity of the tyrosyl residues.…”

Section: Introductionmentioning

confidence: 96%

Quenching of Tyrosine Fluorescence by Phosphate Ions: A Model Study for Protein‐nucleic Acid Complexes

Alev‐Behmoaras

Toulmé

Hélène

1979

Photochem & Photobiology

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Abstract— In order to test the ability of phosphate groups to quench the tyrosine fluorescence in nucleic acid‐protein complexes, we have studied the effect of several phosphate ions on the fluorescence of tyrosine derivatives. Mono and bianions (H2PO4 and HPO42–) which are good proton acceptors quenched the fluorescence of all the phenolic compounds studied except that of O‐methyl tyrosine. With the other derivatives (tyrosine, N‐acetyl tyrosinamide and lysyl‐tyrosyl‐α lysine) fluorescence inhibition was accompanied by the appearance of a long wavelength emission (345 nm) attributed to tyrosinate anions. The quenching of tyrosine emission was due to the deprotonation of the phenolic group promoted in the excited state by phosphate ions and leading to the weakly fluorescent tyrosinate ion. Mono and dianions of phosphate mono ester inhibited tyrosine fluorescence as did unesterified phosphates. However, phosphate diester did not have any effect on the fluorescence of tyrosine derivatives. We conclude from this study that in nucleic acid‐protein complexes phosphate groups are not able to quench tyrosine fluorescence except at the end of polynucleotide chains. Since monoester and diester monoanions have a different behavior, we propose that quenching of tyrosine fluorescence by monoanions requires the formation of two hydrogen bonds. This complex cannot form with diesters which consequently do not quench tyrosine fluorescence.

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Interaction of Disulfide Groups With Nucleic Acid Bases

Cited by 14 publications

References 24 publications

Interaction between the lac operator and the lac repressor headpiece: fluorescence and circular dichroism studies.

Interaction between the lac operator and the lac repressor headpiece: fluorescence and circular dichroism studies.

Cross-Linking of Proteins to Nucleic Acids by Ultraviolet Light

Quenching of Tyrosine Fluorescence by Phosphate Ions: A Model Study for Protein‐nucleic Acid Complexes

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