Purification and functional roles of the P I and P II components of Escherichia coli glutamine synthetase deadenylylation system
Autor: | Earl R. Stadtman, Wayne B. Anderson |
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Rok vydání: | 1971 |
Předmět: |
Stereochemistry
Uracil Nucleotides Glutamine Biophysics Biology medicine.disease_cause Biochemistry Catalysis Phosphates Ligases chemistry.chemical_compound Adenosine Triphosphate Bacterial Proteins Glutamine synthetase Pi medicine Escherichia coli Methods Chemical Precipitation Protamines Molecular Biology Carbon Isotopes Manganese Ethanol Effector Adenine Nucleotides Nucleotides Sulfates RNA Phosphorus Isotopes Sulfuric Acids Nucleotidyltransferases Quaternary Ammonium Compounds chemistry Solubility Chromatography Gel Ketoglutaric Acids Adsorption |
Zdroj: | Archives of biochemistry and biophysics. 143(2) |
ISSN: | 0003-9861 |
Popis: | The deadenylylation of glutamine synthetase is catalyzed by the combined action of two, easily separable, protein components (P I and P II ). The P I component by itself catalyzes slow deadenylylation when it is adsorbed onto manganese phosphate precipitate. The response of this “solid phase” [P I -Mn-PO 4 ]-catalyzed deadenylylation reaction to various effectors is very different from that exhibited by the reaction catalyzed by a soluble mixture of P I and P II . Thus, the P I -P II system is activated by ATP, UTP, α-ketoglutarate, RNA, and ethanol and is inhibited by glutamine, whereas the [P I -Mn-PO 4 ] 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 P I and P II is significantly different from that observed earlier by Shapiro (13) for relatively impure preparations. The results are compatible with the interpretation that the P II component is concerned with the regulation of deadenylylation activity. This and alternative possibilities are discussed. |
Databáze: | OpenAIRE |
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