Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase.

Kingdon, Henry S.; Shapiro, Bennett M.; Stadtman, Earl R.

doi:10.1073/pnas.58.4.1703

Cited by 188 publications

(99 citation statements)

References 7 publications

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“…Stadtman and colleagues (109,120,376) and Holzer et al (377) observed that adenylylated GS is generally (much) more sensitive to feedback inhibitors than unadenylylated GS. In hindsight, early results obtained regarding feedback inhibition were confounded by the fact that the cultivation method and the growth phase of cells used to obtain GS preparations affected the adenylylation state of GS and, hence, the level of inhibition (120,377).…”

Section: Kinetic Regulationmentioning

confidence: 99%

“…The nitrogen status of the cell, as signaled by glutamine and 2-oxoglutarate, regulates the activity of GS. Although glutamine does not inhibit E. coli GS activity directly (see above), it exerts indirect control via signal transduction through the enzyme adenylyltransferase (ATase): it reduces the activity of GS by causing covalent modification, i.e., a covalent linkage of an AMP group to each subunit of GS (109,115,378). ATase is also able to deadenylylate GS-AMP (83,90) (Fig.…”

Section: Signal Transduction-mediated Regulationmentioning

confidence: 99%

“…ATase reduces the activity of GS by covalent modification, i.e., by the covalent linkage of an AMP group to each GS subunit, using ATP as an AMP donor and with the release of pyrophosphate (PP i ) (82,(108)(109)(110) (Table 4). Each subunit of GS can be adenylylated so that one molecule of GS 12 can have 12 AMP groups covalently attached (GS 12 -AMP 12 ).…”

Section: Adenylyltransferase/adenylyl-removing Enzymementioning

confidence: 99%

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Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

Heeswijk¹,

Westerhoff

Boogerd³

2013

Microbiol Mol Biol Rev

228

246

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SUMMARY We present a comprehensive overview of the hierarchical network of intracellular processes revolving around central nitrogen metabolism in Escherichia coli . The hierarchy intertwines transport, metabolism, signaling leading to posttranslational modification, and transcription. The protein components of the network include an ammonium transporter (AmtB), a glutamine transporter (GlnHPQ), two ammonium assimilation pathways (glutamine synthetase [GS]-glutamate synthase [glutamine 2-oxoglutarate amidotransferase {GOGAT}] and glutamate dehydrogenase [GDH]), the two bifunctional enzymes adenylyl transferase/adenylyl-removing enzyme (ATase) and uridylyl transferase/uridylyl-removing enzyme (UTase), the two trimeric signal transduction proteins (GlnB and GlnK), the two-component regulatory system composed of the histidine protein kinase nitrogen regulator II (NRII) and the response nitrogen regulator I (NRI), three global transcriptional regulators called nitrogen assimilation control (Nac) protein, leucine-responsive regulatory protein (Lrp), and cyclic AMP (cAMP) receptor protein (Crp), the glutaminases, and the nitrogen-phosphotransferase system. First, the structural and molecular knowledge on these proteins is reviewed. Thereafter, the activities of the components as they engage together in transport, metabolism, signal transduction, and transcription and their regulation are discussed. Next, old and new molecular data and physiological data are put into a common perspective on integral cellular functioning, especially with the aim of resolving counterintuitive or paradoxical processes featured in nitrogen assimilation. Finally, we articulate what still remains to be discovered and what general lessons can be learned from the vast amounts of data that are available now.

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Section: Kinetic Regulationmentioning

confidence: 99%

Section: Signal Transduction-mediated Regulationmentioning

confidence: 99%

Section: Adenylyltransferase/adenylyl-removing Enzymementioning

confidence: 99%

See 1 more Smart Citation

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

Heeswijk¹,

Westerhoff

Boogerd³

2013

Microbiol Mol Biol Rev

228

246

View full text Add to dashboard Cite

show abstract

“…This result is similar to that observed in adenylylation of E. coli GS. 35,36) The activity ratio in the extract of cells before the addition of ammonia was almost the same as that in the extract of cells grown for 30 h, and the ratio after the addition of ammonia was similar to that in the extract of cells grown for 60 h (data not shown).…”

Section: Adenylylation Of Gs In P Taetrolens Y-30mentioning

confidence: 70%

Cloning and Expression ofPseudomonas taetrolensY-30 Gene Encoding Glutamine Synthetase: An Enzyme Available for Theanine Production by Coupled Fermentation with Energy Transfer

Yamamoto

Wakayama

Tachiki

2006

Bioscience, Biotechnology, and Biochemistry

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“…Three different ATase preparations were used: (1) Fractions from the hydroxyapatite column described in Fig. 3 chromatographic separations on hydroxyapatite there appeared to have been some conversion to a form that retains ATase activity but is without PI-DA activity.…”

mentioning

confidence: 99%

Adenosine Triphosphate: Glutamine Synthetase Adenylyltransferase of Escherichia coli: Two Active Molecular Forms

Hennig

Anderson

Ginsburg

1970

Proc. Natl. Acad. Sci. U.S.A.

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Abstract. Two active forms of purified ATP :glutamine synthetase adenylyltransferase from Escherichia coli are apparent on polyacrylamide gel electrophoresis at pH 8. The slower migrating component, which is identical to the PI-protein fraction of the glutamine synthetase deadenylylating enzyme system, has s20, -5.1 S and a molecular weight of about 130,000. The more rapidly migrating adenylyltransferase component has s20, --4.0 S and a molecular weight of about 70,000. During storage at 4VC, the larger adenylyltransferase component (PI) converts to the smaller active unit with a concomitant loss of both PI deadenylylating activity and soluble protein. It is concluded that the low-molecular weight form of the adenylyltransferase is a subunit of the deadenylylating PI-protein.The ATP: glutamine synthetase adenylyltransferase (ATase) is a part of an elaborate system for the regulation of glutamine synthetase activity in Escherichia coli.1-6 The adenylyltransferase catalyzes the covalent attachment of a 5'-adenylyl group to each of the 12 subunits of glutamine synthetase2'3'5-8 and thereby markedly changes the catalytic and regulatory characteristics of the synthetase.'-0 The 5'-adenylyl group is esterified in phosphodiester linkage to the phenolic hydroxyl moiety of a specific tyrosyl residue of the subunit polypeptide chain."'12 In E. coli, there exists also a complex deadenylylating enzyme system that specifically catalyzes the removal of 5'-adenylyl groups from glutamine synthetase.53 1314 Ebner et al.'-recently described the purification and some properties of ATase from E. coli B, whereas an ATase of low molecular weight was isolated from E. coli W in this laboratory'6. Except for its smaller size, many characteristics of the enzyme from the W strain were similar to those of the enzyme studied in Holzer's laboratory.6" 5"l7 The studies of Anderson et al.'8 and the present report show that ATase activity can be associated with the PI-protein fraction of the deadenylylating enzyme system. This communication gives information on the relationship of the two active molecular forms of ATase obtained during the purification of this enzyme. Materials and Methods. Three different ATase preparations were used: (1) Fractions from the hydroxyapatite column described in Fig. 3 of ref. 18, containing >400 units ATase per mg protein, were combined and dialyzed against 10 mM potassium 1761

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Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase.

Cited by 188 publications

References 7 publications

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

Cloning and Expression ofPseudomonas taetrolensY-30 Gene Encoding Glutamine Synthetase: An Enzyme Available for Theanine Production by Coupled Fermentation with Energy Transfer

Adenosine Triphosphate: Glutamine Synthetase Adenylyltransferase of Escherichia coli: Two Active Molecular Forms

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