Interactions of aromatic residues of proteins with nucleic acids. Fluorescence studies of the binding of oligopeptides containing tryptophan and tyrosine residues to polynucleotides

Brun, Francine; Toulmé, Jean Jacques; Hélène, Claude

doi:10.1021/bi00674a015

Cited by 229 publications

(147 citation statements)

References 8 publications

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“…Stacking interaction of tryptophan with nucleic acid bases has been well established by investigators using oligopeptides containing tryptophan [19,20]. Since the stacking interaction has been shown to lead to a quenching of tryptophan fluorescence, the present result of fluorescence enhancement suggests that stacking of Trp-211 with adenine does not take place.…”

Section: Discussionmentioning

confidence: 81%

Fluorescence studies on the interaction of adenine with ricin A‐chain

1992

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Ricin A.chain, an N-glycosidase that attacks 28S rRNA at a highly conserved adenine residue, has a unique tryptophan (Trp-211) in the putative active site cleft, Fluorescence spectroscopy revealed that specific binding oi" adenine to the A.chain caused a large enhancement of Trp-211 fluorescence (70%) arid a concomitant red shift of the emission spectrum (8 am). A Scatehard plot of the fluorescence enhancement data ~,vas not linear, indicating that the environment ofTrp-211 was altered by heterogeneous binding of adenines, These results, taken tol~ether with the protective effect of adenine on the ribosome-inactivation by riein A-chain, suggest that at least two adenines bind to the active site cleft, Riein A-chain; Adenine-protein interaction; Active site; Tryptophan fluorescence; Ribosome inactivation

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Section: Discussionmentioning

confidence: 81%

Fluorescence studies on the interaction of adenine with ricin A‐chain

1992

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“…A plane formed by an aromatic ring of tryptophan or tyrosine in its binding pocket may be sufficient for hMTH1 to bind to 2-OH-A, whereas the indole ring of tryptophan might serve as an essential structure for its recognition of 8-oxoG. In general, tryptophan and other amino acid residues with aromatic side chains present in a substrate binding pocket have an electrostatic effect on stacking a purine ring by their -interactions (38). It is likely that the unique structural features of 8-oxoG, N7-H/C8ϭO or N7/ C8-OH, maximize the favorable interaction between the purine and indole rings.…”

Section: Discussionmentioning

confidence: 99%

A Molecular Basis for the Selective Recognition of 2-Hydroxy-dATP and 8-Oxo-dGTP by Human MTH1

Sakai¹,

Furuichi²,

Takahashi³

et al. 2002

Journal of Biological Chemistry

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MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxydATP, and 2-hydroxy rATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration. This substrate specificity for oxidized purine nucleoside triphosphates was investigated by mutation analyses based on the sequence comparison with the Escherichia coli homolog, MutT, which hydrolyzes only 8-oxo-dGTP and 8-oxo-rGTP but not oxidized forms of dATP or ATP. Neither a replacement of the phosphohydrolase module of MTH1 with that of MutT nor deletions of the C-terminal region of MTH1, which is unique for MTH1, altered the substrate specificity of MTH1. In contrast, the substitution of residues at position Trp-117 and Asp-119 of MTH1, which showed apparent chemical shift perturbations with 8-oxo-dGDP in NMR analyses but are not conserved in MutT, affected the substrate specificity. Trp-117 is essential for MTH1 to recognize both 8-oxodGTP and 2-hydroxy-dATP, whereas Asp-119 is only essential for recognizing 2-hydroxy-dATP, thus suggesting that origins of the substrate-binding pockets for MTH1 and MutT are different.Endogenous oxidation of nucleic acids, such as DNA, RNA, and their precursors by reactive oxygen species generated under normal metabolic conditions, appear to induce spontaneous mutagenesis and cell death, which have been implicated in aging and various diseases including cancer and neuronal degeneration (1). It has been established that 8-oxoguanine (8-oxoG), an oxidized form of guanine, is highly mutagenic and one of the main endogenous sources for spontaneous mutagenesis. During DNA replication, 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) can be inserted into the nascent strand opposite adenine and cytosine in the template, with almost equal efficiency, thus resulting in an A:T to C:G transversion mutation (2, 3). Accumulation of 8-oxoG in double-stranded DNA is caused by direct oxidization of guanine in DNA or incorporation of precursor nucleotide, 8-oxo-dGTP, which is generated in nucleotide pools with oxidation of dGTP (4). A misincorporation of oxidized nucleotides also occurs during transcription, thus leading to an accumulation of abnormal proteins (5, 6).To eliminate such deleterious oxidized nucleotides, organisms come equipped with elaborate mechanisms. In Escherichia coli the MutT protein hydrolyzes 8-oxo-dGTP and 8-oxoguanosine triphosphate (8-oxo-rGTP) to the monophosphate form, thus avoiding the misincorporation of mutagenic nucleotides into DNA and mRNA during replication and transcription (7,8). The absence of the mutT gene increases the spontaneous occurrence of A:T to C:G transversion a thousandfold over the wild type level (7, 9), and further increases the occurrence of transcriptional errors (6). Enzymatic activities similar to that of MutT had been identified in both human and other mammalian cells (10 -13). Based on the similarity in their amino acid sequences to that of Mut...

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“…The tripeptide LysTrpLys binds to DNA [6,7] and to single stranded polynucleotides [4,5] Both complexes involve electrostatic interactions between the phosphate groups of the nucleic acid and the amino groups of the lysyl residues of the peptide. In complex I the fluorescence quantum yield of tryptophan is identical to that of the free peptide.…”

Section: Introductionmentioning

confidence: 99%

“…Complex II involves a stacking of the tryptophanyl ring with the nucleic acid bases and the fluorescence of the peptide is completely quenched. The value of K2, which represents the ratio of the concentrations of stacked to unstacked complexes, is much smaller for double stranded than for single stranded nucleic acids [4,6,7].…”

Section: Introductionmentioning

confidence: 99%