Authentic Edition of Sonata, A Major (K. 331); Fantasy, D Minor (K. 397); Sonata, G Major (K. 283); Rondo, D Major (K. 485)

Jacobson, Winifred; Mozart, Wolfgang Amadeus

doi:10.2307/893376

Cited by 9 publications

(13 citation statements)

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“…No apparent RNA or 'oligonucleotide' was present, and our analysis of nascent DNA chains after alkali treatment had revealed that all four deoxyribonucleoside monophosphates were present at the 5' end in approximately equal amounts [27]. This result had also been obtained by other investigators [7,10]. We thought it necessary, though, to extend this analysis to determine further the influence of pulse-labeling and lysing conditions on the nature of the 5' ends.…”

Section: Nature Of 5' Ends Of' Dna Chainssupporting

confidence: 70%

“…Third, post-replication repair processes also complicate studies on DNA replication bccause of the similar properties of D N A chains that arise through replication and those that arise through repair [14,15].Another factor which often renders the study of DNA replication difficult concerns non-nascent DNA chains. The cell contains a large number of short D N A chains which originate outside the replication fork [7,16,17]. Many of the techniques used to purify nascent DNA d o not distinguish between nascent and non-nascent chains and, as a result, the non-replicative chains are isolated togethcr with the replication intermediates.…”

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confidence: 99%

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Origin and Characterization of Short DNA Chains in Escherichia coli

Siegmann

Werner

1981

European Journal of Biochemistry

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One of the major problems in the study of DNA replication involves the presence of numerous short, nonnascent DNA chains in the cell. Such chains often contaminate nascent D N A preparations, making accurate analysis of the replicative DNA difficult. This complication can be avoided by the use of hydroxyapatite chromatography. Previous results from this laboratory had shown that short nascent DNA chains could be eluted from hydroxyapatite at low phosphate concentrations because of their non-covalent association with protein. Additional data now indicate that this isolation procedure yields a DNA preparation which contains only nascent DNA and is essentially free of non-nascent chains. 5'-Terminal labeling patterns and molecular weight distributions show that only nascent DNA chains form the DNA-protein complex and can therefore be separated from non-nascent chains if the isolation is performed under non-denaturing conditions. The protein involved in the complex appears to be rather specific for DNA chains in the replication fork since short chains resulting from the excision of dUMP immediately after replication also form the DNA-protein complcx.Using this isolation technique, the 5'-terminal nucleotides of nascent DNA chains were determined in an effort to learn something about the chain initiation process. DNA was pulse-labeled in several ways, purified by hydroxyapatite chromatography, and labeled at the 5' end with [32P]phosphate. Two-dimensional thin-layer chromatography of the 32P-labeled nucleotides, obtained after enzymatic hydrolysis, revealed that all four deoxyribonucleotides are present at the 5' end in approximately equal amounts. In most cases, this 5'-terminal nucleotide distribution does not vary significantly, even when the conditions of pulse-labeling are changed. Only if the cells are allowed to run out of thymine is a variation in the relative amounts of 5'-end nucleotides detected. In this case, the amount of dTMP at the 5' end decreases significantly, reflecting the low thymine levels and indicating that the cell can compensate for this deficiency by utilizing other available nucleotides. From these results, it appears that DNA chain initiation is essentially random with respect to the nucleotide used in the initiation process.Because of its fundamental importance, the process of DNA replication has been studied extensively. However, some of the basic aspects of the replication mechanism, such as DNA chain initiation at the replication fork, are still not fully understood, and often different laboratories report conflicting results [I -101. There are several possible reasons for the varying results that are obtained. First, different DNA precursors and different methods of pulse-labeling the D N A have been shown to produce different labeling patterns, indicating that the mode of DNA replication is subject to external influences and disruptions, and suggesting that several related processes may occur simultaneously with replication [7, 11 -131. Second, the different methods used to isolate ...

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Section: Nature Of 5' Ends Of' Dna Chainssupporting

confidence: 70%

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confidence: 99%

Origin and Characterization of Short DNA Chains in Escherichia coli

Siegmann

Werner

1981

European Journal of Biochemistry

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“…It has also been shown that Li+ strongly affects phosphatidylserine bilayers [16]. However, monovalent cations do not appear to produce any appreciable effects on the properties of electrically neutral phospholipids [14,17]. This is further supported by Fig.6, showing that the area per polar head group is rather insensitive to addition of monovalent ions.…”

Section: Discussionmentioning

confidence: 69%

The Interactions between Monovalent Ions and Phosphatidyl Cholines in Aqueous Bilayers

Söderman¹,

Arvidson²,

Lindblom

et al. 1983

European Journal of Biochemistry

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The interactions of lithium and sodium ions and water with phosphatidylcholine bilayers have been studied by means of 7Li, 23Na and 'H NMR quadrupole splittings. The experimental results are interpreted in terms of a simple three-site model with two anisotropic sites ('binding' sites) and one isotropic site ('free' ions and water molecules). The findings obtained for the zwitterionic model membrane are compared with previous investigations of lamellar phases composed of ionic and nonionic amphiphiles. It is shown that the data obtained are compatible with our previous suggestion [Lindblom, G., Persson, N.-O., and Arvidson G. (2976) Adv. Chem. Ser. 152, 1211 that an increase in the salt content in the water layer induces a conformational change in the polar head group of phosphatidylcholine. Thus at high salt concentration the phosphocholine head group tends to be oriented perpendicular to the lipid bilayer surface. The study also shows that increasing the amount of salt leads to a squeezing out of water between the bilayers. This is interpreted in terms of a reduction of the repulsion forces between the bilayers.The basic structure of most biological membranes is a phospholipid bilayer. Soap/water and phospholipid/water systems, forming lipid bilayers of defined compositions, have therefore been used extensively as models in membrane studies. Interaction between inorganic ions and biological membranes plays an important role in cell function and numerous studies have been performed on the interaction between ions and phospholipid membranes (see [I] and references therein). Recently, it has also been shown that monovalent cations can bind to phospholipid membranes, especially to highly charged phosphatidyl serine membranes Since the most abundant inorganic cations in living systems are the alkali ions, a thorough understanding of the interactions between such ions and the different models used in membrane studies is needed. Therefore, we have for some time investigated, both theoretically and experimentally, the interaction between monovalent ions and simple soap/water bilayers [3-81. This work has shown that the direct monitoring of the ions interacting with the bilayer through their quadrupole splittings, as measured by NMR, can give information about ion binding in membrane systems. Here we have performed an NMR and X-ray study on the effect of LiCl in model systems composed of unsaturated phosphatidylcholines. PI.Abbreviations. OlezGro-P-Cho, 1,2-dioleoyl-sn-glycero-3-phosphocholine; PamOleGro-P-Cho, l-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine; PtdCho, phosphatidyl choline; PamzGro-P-Cho, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine; Myr2Gro-P-Cho, 2,2-dimyristoyl-snglycero-3-phosphocholine.

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“…On the other hand, not only does the PMA analog 4-cr-PDD not inhibit the effect of fMet-Leu-Phe, but it apparently potentiates it. Though unexplained at present, this effect of ~-cx-PDD may be the result of the highly hydrophobic nature of 4+PDD [21]. It is worthwhile noting that the basal activity of the GTPase was also inhibited by pretreatment of the cells with PMA.…”

Section: Resultsmentioning

confidence: 86%

Treatment of rabbit neutrophils with phorbol esters results in increased ADP‐ribosylation catalyzed by pertussis toxin and inhibition of the GTPase stimulated by fMet‐Leu‐Phe

et al. 1986

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The effects of pretreatment of rabbit neutrophils with phorbol 12-myristate 13-acetate on the ability of pertussis toxin to catalyze ADP-ribosylation and of fMet-Leu-Phe to activate a high-affinity GTPase in these cell homogenates were examined. The addition of phorbol 12-myristate 13-acetate, but not 4cr-phorbol 12,13-didecanoate, to intact cells was found to stimulate by more than 100% the pertussis toxin-dependent ribosylation of a 41 kDa protein (either the cc-subunit of the 'inhibitory' guanine nucleotide-binding protein N, or a closely analogous protein) and to inhibit by more than 60% the activation by fMet-Leu-Phe of the GTPase of the neutrophil homogenates.The addition of fMet-Leu-Phe to intact cells increases the ADPribosylation catalyzed by pertussis toxin of the 41 kDa protein. On the other hand, the exposure of neutrophi1 homogenates to fMet-Leu-Phe results in a decreased level of ADP-ribosylation. This decreased ribosylation reflects a dissociation of the GTP-binding protein oligomer that is not followed by association. possibly because of the release of the a-subunit into the suspending media. The implications of these results for the understanding of the mechanism of inhibition of cell responsiveness by phorbol esters and the heterologous desensitization phenomenon are discussed. Prominent among these are the possibilities that (i) the rate of dissociation of the N, oligomer is affected by the degree of its phosphorylation by protein kinase C, and/or (ii) the dissociated phosphorylated a-subunit (the 41 kDa protein) is functionally less active than its dephosphorylated couterpart. Phorbol ester Pertussis toxin ADP-ribosylation

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Authentic Edition of Sonata, A Major (K. 331); Fantasy, D Minor (K. 397); Sonata, G Major (K. 283); Rondo, D Major (K. 485)

Cited by 9 publications

References 0 publications

Origin and Characterization of Short DNA Chains in Escherichia coli

Origin and Characterization of Short DNA Chains in Escherichia coli

The Interactions between Monovalent Ions and Phosphatidyl Cholines in Aqueous Bilayers

Treatment of rabbit neutrophils with phorbol esters results in increased ADP‐ribosylation catalyzed by pertussis toxin and inhibition of the GTPase stimulated by fMet‐Leu‐Phe

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