Ligand-Induced Conformational Changes in Ribonucleic Acids

Gassen, Hans Günter

doi:10.1016/s0079-6603(08)60671-6

Cited by 35 publications

(13 citation statements)

References 111 publications

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“…The essential role played by Mg2+ ions in translation complexes has been repeatedly stressed. Mg2+ is required for structural integrity of ribosomal particles and an efficient translational process (Gassen, 1980). Mg2+ stabilizes the association of the ribosomal subunits (Weiss et al, 1973;Zamir et al, 1971;Stahli et al, 1977; Wishnia & Boussert, 1977;Shimmel & Redfield, 1980), the tertiary structure of tRNA (Stein & Crothers, 1976;Jack et al, 1977), and the codon-TIME, s figure 6: Displacement of VS bound to ribosomes by erythromycin.…”

Section: Discussionmentioning

confidence: 99%

Interaction between virginiamycin S and ribosomes is partly provided by a salt bridge with a magnesium ion

Giambattista¹,

Engelborghs²,

Nyssen³

et al. 1991

Biochemistry

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Type B streptogramins, such as virginiamycin S (VS), are cyclic hexadepsipeptides, inhibiting protein synthesis in prokaryotes. L-Thr connects a 3-hydroxypicolinyl residue (3-OH-Pic) to the peptide lactone ring. The fluorescence intensity of 3-OH-Pic is strongly increased by chelation to alkaline earth cations or binding to ribosomes. Similar behavior of the ribosome-VS complex and the VS-Mg chelate provides strong evidence for the presence of a VS-Mg chelate within the ribosomal binding site. Different models involving the ribosome binding of either members of the VS-Mg2+ chelate or both have been tested by fluorescence lifetime measurements, equilibrium titrations, and stopped-flow spectrofluorometry. Our data strongly suggest that (a) the interaction between VS and the ribosome is partly provided by a salt bridge between suitable acceptor atoms of the ribosome and the 3-OH-Pic residue, (b) Mg2+ can be exchanged by Mn2+ without dissociation of the ribosome-VS complex, (c) Mg2+ coordinates to the negative form of the 3-OH-Pic residue, probably via an interaction with the phenolate oxygen and the amide carboxyl group, and (d) the picolinyl residue is essential for the biological activity, as indicated by the lack of activity when the latter is replaced by a serine derivative.

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Section: Discussionmentioning

confidence: 99%

Interaction between virginiamycin S and ribosomes is partly provided by a salt bridge with a magnesium ion

Giambattista¹,

Engelborghs²,

Nyssen³

et al. 1991

Biochemistry

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“…It has been known that Mg2+ ions are required for protein synthesis and tRNAs must be a structurally flexibe to perform many functions (32). In the previous paper, we suggested thatthe removal ofMg 2 + atlow monovalent cation concentration oflO mM K+ causes a significant decrease in the distance between 3' -terminus and anticodon by the energy transfer measurement (1~ The present data demonstrate the conformational change of the L-shaped tRNA e in the presence of 100 mM K+ and 10 mM Mi+.…”

Section: Discussionmentioning

confidence: 99%

Conformational Change of the L-Shaped tRNA^PheMolecule

Nagamatsu

1989

Journal of Biomolecular Structure and Dynamics

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Fluorophore of proflavine was introduced onto the 3'-terminal ribose moiety of yeast tRNA(Phe). The distance between the fluorophore and the fluorescent Y base in the anticodon of yeast tRNA(Phe) was measured by a singlet-singlet energy transfer. Conformational changes of tRNA(Phe) with binding of tRNA(2Glu), which has the anticodon UUC complementary to the anticodon GAA of tRNA(Phe), were investigated. The distance obtained at the ionic strength of 100 mM K+ and 10 mM Mg2+ is very close to the distance from x-ray diffraction, while the distance obtained in the presence of tRNA(2Glu) is significantly smaller. Further, using a fluorescent probe of 4-bromomethyl-7-methoxycoumarin introduced onto pseudouridine residue psi 55 in the T psi C loop of tRNA(Phe), Stern-Volmer quenching experiments for the probe with or without added tRNA(2Glu) were carried out. The results showed greater access of the probe to the quencher with added tRNA(2Glu). These results suggest that both arms of the L-shaped tRNA structure tend to bend inside with binding of tRNA(2Glu) and some structural collapse occurs at the corner of the L-shaped structure.

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“…Specific models for structural interactions and possible conformational changes during the tRNA-ribosome recognition process are reviewed by Ofengand et al (1980); see also Gassen (1980) and Thompson and Hearst (1983).…”

Section: Function Of Trnamentioning

confidence: 99%

“…Resonance broadening of the D16 and D17 C6 proton NMR signals upon complex formation has been interpreted as a conformational change in the central portion of the L of yeast tRNA (Davanloo et al, 1979;Geerdes et al, 1980b). Further evidence for such an allosteric effect is reviewed by Gassen (1980) and Rigler and Wintermeyer (1983). Gueron et al (1983) recently proposed that the asymmetry can be ascribed to interference between dipolar and chemical shift anisotropy relaxation mechanisms (see below for a discussion of these mechanisms).…”

Section: Saturation Recovery Of Magnetization For Individual Exchangementioning

confidence: 99%

19F NMR studies of the solution structure and dynamics of 5-fluorouracil-substituted valine tRNA from Escherichia coli

Hardin

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Ligand-Induced Conformational Changes in Ribonucleic Acids

Cited by 35 publications

References 111 publications

Interaction between virginiamycin S and ribosomes is partly provided by a salt bridge with a magnesium ion

Interaction between virginiamycin S and ribosomes is partly provided by a salt bridge with a magnesium ion

Conformational Change of the L-Shaped tRNA^PheMolecule

19F NMR studies of the solution structure and dynamics of 5-fluorouracil-substituted valine tRNA from Escherichia coli

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Ligand-Induced Conformational Changes in Ribonucleic Acids

Cited by 35 publications

References 111 publications

Interaction between virginiamycin S and ribosomes is partly provided by a salt bridge with a magnesium ion

Interaction between virginiamycin S and ribosomes is partly provided by a salt bridge with a magnesium ion

Conformational Change of the L-Shaped tRNAPheMolecule

19F NMR studies of the solution structure and dynamics of 5-fluorouracil-substituted valine tRNA from Escherichia coli

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Conformational Change of the L-Shaped tRNA^PheMolecule