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- W2067079368 abstract "Exponentially growing cells of Escherichia coli, subjected to a simultaneous temperature and osmotic shock are capable of carrying out exchange between inorganic phosphate and ribonucleoside 5′-polyphosphate. The exchange reaction carried out by shocked cells is judged to be catalysed by polynucleotide phosphorylase (polyribonucleotide: orthophosphate nucleotidyltransferase, EC 2.7.7.8) for the following reasons: 1. Exchange occurs with ribonucleoside 5′-diphosphate and leads to labeling of only the β-phosphate residue. 2. Exchange labeling of ribonucleoside 5′-triphosphate requires hydrolysis of the β-γ phosphodiester bond and again results in labeling of only the β-phosphate position. With the exception of ATP no label can be detected in the γ-phosphate position of exchange-labeled ribonucleoside 5′-triphosphate. 3. Known inhibitors of polynucleotide phosphorylase interfere with the exchange reaction in shocked cells. 4. Shocked cells from strains carrying a mutation resulting in low levels of polynucleotide phosphorylase activity show an analogous decrease in exchange activity. Experiments on the existence of possible residual permeability restrictions to nucleotides in shocked cells indicate that restrictions still do exist for certain nucleotides." @default.
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- W2067079368 date "1974-02-01" @default.
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- W2067079368 title "Regulation of RNA synthesis in Escherichia coli. II. Polynucleotide phosphorylase activity in cold-shocked cells" @default.
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- W2067079368 doi "https://doi.org/10.1016/0005-2787(74)90172-5" @default.
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