ArticleThe EMBO journal1997
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 102 citations in OpenAlex.
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- The rise of AMPylation: from bacterial beginnings to modern implications in health and disease.Biochemical Society transactions · 2025Review
- Molecular Mechanism and Agricultural Application of the NifA-NifL System for Nitrogen Fixation.International journal of molecular sciences · 2023Review
- Control of nitrogen fixation and ammonia excretion in Azorhizobium caulinodans.PLoS genetics · 2022Article
- Engineering Posttranslational Regulation of Glutamine Synthetase for Controllable Ammonia Production in the Plant Symbiont Azospirillum brasilense.Applied and environmental microbiology · 2021Article
- Fic and non-Fic AMPylases: protein AMPylation in metazoans.Open biology · 2021Article
- Metabolic engineering of Escherichia coli for efficient production of L-alanyl-L-glutamine.Microbial cell factories · 2020Article
- Enzymes Involved in AMPylation and deAMPylation.Chemical reviews · 2018Review
- rAMPing Up Stress Signaling: Protein AMPylation in Metazoans.Trends in cell biology · 2017Review
- GlnK Facilitates the Dynamic Regulation of Bacterial Nitrogen Assimilation.Biophysical journal · 2017Article
- In silico identification of AMPylating enzymes and study of their divergent evolution.Scientific reports · 2015Article
- Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective.Microbiology and molecular biology reviews : MMBR · 2013Review
- Sensitivity and robustness in covalent modification cycles with a bifunctional converter enzyme.Biophysical journal · 2013Article
- Metabolic Regulation of a Bacterial Cell System with Emphasis on Escherichia coli Metabolism.ISRN biochemistry · 2013Review
- Mutagenesis and functional characterization of the four domains of GlnD, a bifunctional nitrogen sensor protein.Journal of bacteriology · 2010Article
- Metabolic regulation of Escherichia coli and its gdhA, glnL, gltB, D mutants under different carbon and nitrogen limitations in the continuous culture.Microbial cell factories · 2010Article
- Reconstitution of Escherichia coli glutamine synthetase adenylyltransferase from N-terminal and C-terminal fragments of the enzyme.Biochemistry · 2009Article
- Functional analysis of GlnE, an essential adenylyl transferase in Mycobacterium tuberculosis.Journal of bacteriology · 2008Article
- In vitro studies of the uridylylation of the three PII protein paralogs from Rhodospirillum rubrum: the transferase activity of R. rubrum GlnD is regulated by alpha-ketoglutarate and divalent cations but not by glutamine.Journal of bacteriology · 2007Article
- Integration of regulatory signals through involvement of multiple global regulators: control of the Escherichia coli gltBDF operon by Lrp, IHF, Crp, and ArgR.BMC microbiology · 2007Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1-423 (AT-N) and 425-945 (AT-C). We demonstrate that ATase has two active sites; AT-N carries a deadenylylation activity and AT-C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT-C domain, whereas alpha-ketoglutarate activates the deadenylylation reaction catalysed by the AT-N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT-N depends on PII-UMP and is inhibited by PII. The adenylylation activity of AT-C is independent of PII (or PII-UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed.
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