期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1971
卷号：68
期号：12
页码：2949-2953
DOI：10.1073/pnas.68.12.2949
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Earlier studies showed that two protein components, PI and PII, are concerned with the adenylylation and deadenylylation of Escherichia coli glutamine synthetase (EC 6.3.1.2 ). PI by itself catalyzes both adenylylation and deadenylylation, but its activity is modulated by the PII-protein and by glutamine, 2-oxoglutarate, ATP, and UTP, The PII-protein exists in two forms: one form, PII-AT, stimulates PI-catalyzed adenylylation activity in the absence of glutamine and makes this activity very sensitive to inhibition by 2-oxoglutarate; it does not affect deadenylylation activity. The other form, PII-DA, stimulates adenylylation only if glutamine is present, and also stimulates the deadenylylation activity of PI, which is then dependent upon the presence of ATP and 2-oxoglutarate. Conversion of PII-AT to PII-DA requires the presence of UTP, ATP, and 2-oxoglutarate; it is catalyzed by an enzyme present in PI preparations. UTP may be directly involved in this conversion since PII-DA fractions reisolated by filtration through Sephadex G-100 contain small quantities of a bound uridine derivative that lacks the {gamma}-phosphoryl group of UTP. The activity of PII-DA, but not of PII-AT, is destroyed by treatment with snake-venom phosphodiesterase. ATP and 2-oxoglutarate apparently function as allosteric effectors for the conversion of PII-AT to PI-DA.
