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- W2069135890 abstract "The deadenylylation of glutamine synthetase is catalyzed by the combined action of two, easily separable, protein components (PI and PII). The PI component by itself catalyzes slow deadenylylation when it is adsorbed onto manganese phosphate precipitate. The response of this “solid phase” [PI-Mn-PO4]-catalyzed deadenylylation reaction to various effectors is very different from that exhibited by the reaction catalyzed by a soluble mixture of PI and PII. Thus, the PI-PII system is activated by ATP, UTP, α-ketoglutarate, RNA, and ethanol and is inhibited by glutamine, whereas the [PI-Mn-PO4] system is inhibited by all these effectors except glutamine and ATP which are without effect. Though qualitatively the same, the relative effectiveness of the various effectors in modulating activity of highly purified mixtures of PI and PII is significantly different from that observed earlier by Shapiro (13) for relatively impure preparations. The results are compatible with the interpretation that the PII component is concerned with the regulation of deadenylylation activity. This and alternative possibilities are discussed." @default.
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- W2069135890 date "1971-04-01" @default.
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- W2069135890 title "Purification and functional roles of the PI and PII components of Escherichia coli glutamine synthetase deadenylylation system" @default.
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- W2069135890 doi "https://doi.org/10.1016/0003-9861(71)90229-3" @default.
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