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Proteins from the prokaryotic nucleoid: 1H NMR study of the quaternary structure of Escherichia coli DNA binding protein NS (HU)
No full textThe quaternary interactions of Escherichia coli DNA binding proteins NS1, NS2, and NS (NS1 + NS2) have been studied by 1H NMR spectroscopy at 400 MHz following the reversible spectral changes produced by temperature increases on the resonances (Phe ring and His C-2 protons) whose spectral characteristics reflect the formation and dissociation of either homologous or heterologous interactions. These changes include (a) a progressive intensity decrease of the Phe resonances shifted to high field by stacking interactions, (b) a progressive intensity increase of the resonances due to freely rotating Phe, and (c) splitting of the His C-2 proton resonance. The association constants and thermodynamic parameters for the homologous and heterologous interactions were calculated from the molar fractions of the relevant molecular species by assuming that the above effects are due to the existence of simple association equilibria. It was found that two (out of three) phenylalanine residues of each polypeptide chain are involved in quaternary interactions. Quantitative data concerning the internal mobility and mutual orientations in aggregates of these Phe rings were also obtained. From the calculated association constants, from comparison of these data with recent protein-protein cross-linking results [Losso, M. A., Pawlik, R. T., Canonaco, M. A., & Gualerzi, C. O. (1986) Eur. J. Biochem. 155, 27-32], and from other considerations, we suggest that even though stacking of the Phe rings occurs at the interface between monomers, the temperature-dependent alteration of the Phe spectrum monitors shifts of the dimer in equilibrium tetramer equilibrium whereas the splitting of the His C-2 proton resonance most likely monitors the equilibrium between tetramers and larger aggregates
The interaction between initiation factor 3 and 30 S ribosomal subunits studied by high-resolution 1H NMR spectroscopy
No full textThe interaction between Escherichia coli translational initiation factor 3 (IF-3) (Mr = 20668) and 30 S ribosomal subunits or fragmented 16 S rRNA was followed by 1H NMR spectroscopy. Upon addition of increasing yet largely substoichiometric amounts of deuterated 30 S ribosomal subunits, selective line broadenings and some chemical shift changes were observed. These effects can be fully reversed by increasing the temperature and/or the ionic strength. The selective line broadenings, which are explained by a medium-fast to fast exchange dynamics between free and bound IF-3 with loss of internal mobility of the protons, shed light on the amino acid residues of IF-3 involved in or affected by the binding to the 30 S subunits. Some effects (i.e. implication of 1 tyrosine, 1 phenylalanine, and some arginine and lysine residues) are seen with both 30 S subunits and rRNA while others (i.e. implication of a second tyrosine or phenylalanine residue of a group of hydrophobic residues and, possibly, of the single histidine residue), seen only or preferentially with 30 S subunits, may reflect additional interactions exclusively occurring at the ribosomal level
Mechanical stability of resonant Bose-Fermi mixtures
No full textWe investigate the mechanical stability of Bose-Fermi mixtures at zero temperature in the presence of a tunable Feshbach resonance, which induces a competition between boson condensation and boson-fermion pairing when the boson density is smaller than the fermion density. Using a many-body diagrammatic approach validated by fixed-node Quantum Monte Carlo calculations and supported by recent experimental observations, we determine the minimal amount of boson-boson repulsion required to guarantee the stability of the mixture across the entire range of boson-fermion interactions from weak to strong coupling. Our stability phase diagrams indicate that mixtures with boson-to-fermion mass ratios near two, such as the87 Rb-40 K system, exhibit optimal stability conditions. Moreover, by applying our results to a recent experiment with a23 Na-40 K mixture, we find that the boson-boson repulsion was insufficient to ensure stability, suggesting that the experimental timescale was short enough to avoid mechanical collapse. On the other hand, we also show that even in the absence of boson-boson repulsion, Bose-Fermi mixtures become intrinsically stable beyond a certain coupling strength, preceding the quantum phase transition associated with the vanishing of the bosonic condensate. We thus propose an experimental protocol for observing this quantum phase transition in a mechanically stable configuration
Structure-function relationships in Escherichia coli translational elongation factor G: modification of lysine residues by the site-specific reagent pyridoxal phosphate
No full textTranslation of mRNA with degenerate initiation triplet AUU displays high IF2 dependence and is subject to IF3 repression
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From stand-by to decoding site. Adjustment of the mRNA on the 30S ribosomal subunit under the influence of the initiation factors
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Chemical modification in situ of Escherichia coli 50 S ribosomal proteins by the site-specific reagent pyridoxal phosphate. Inactivation of the elongation factor-G-dependent GTPase and of the association with the small ribosomal subunit
No full textSelective stimulation of translation of leaderless mRNA by IF2: evolutionary implications for translation
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