ArticleJournal of bacteriology2008
Functional analysis of GlnE, an essential adenylyl transferase in Mycobacterium tuberculosis.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Exploring protein adenylyltransferase as a therapeutic target for combating ESKAPE pathogens in hospital-acquired infections.Molecular biology reports · 2025Review
- Molecular Mechanism and Agricultural Application of the NifA-NifL System for Nitrogen Fixation.International journal of molecular sciences · 2023Review
- Nitrogen metabolism in mycobacteria: the key genes and targeted antimicrobials.Frontiers in microbiology · 2023Review
- Polyamine and Ethanolamine Metabolism in Bacteria as an Important Component of Nitrogen Assimilation for Survival and Pathogenicity.Medical sciences (Basel, Switzerland) · 2022Review
- Control of nitrogen fixation and ammonia excretion in Azorhizobium caulinodans.PLoS genetics · 2022Article
- Novel polyadenylylation-dependent neutralization mechanism of the HEPN/MNT toxin/antitoxin system.Nucleic acids research · 2020Article
- Identification of Mycobacterium tuberculosis Peptides in Serum Extracellular Vesicles from Persons with Latent Tuberculosis Infection.Journal of clinical microbiology · 2020Article
- Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis.Nature communications · 2020Article
- Article
- Enzymes Involved in AMPylation and deAMPylation.Chemical reviews · 2018Review
- Phylogenomic exploration of the relationships between strains of Mycobacterium avium subspecies paratuberculosis.BMC genomics · 2016Article
- Deciphering the metabolic response of Mycobacterium tuberculosis to nitrogen stress.Molecular microbiology · 2015Article
- The Transcriptional Repressor, MtrR, of the mtrCDE Efflux Pump Operon of Neisseria gonorrhoeae Can Also Serve as an Activator of "off Target" Gene (glnE) Expression.Antibiotics (Basel, Switzerland) · 2015Article
- Nitrogen metabolism in Mycobacterium tuberculosis physiology and virulence.Nature reviews. Microbiology · 2014Review
- Integrated transcriptomic and proteomic analysis of the bile stress response in a centenarian-originated probiotic Bifidobacterium longum BBMN68.Molecular & cellular proteomics : MCP · 2014Article
- Mycobacterium tuberculosis exploits asparagine to assimilate nitrogen and resist acid stress during infection.PLoS pathogens · 2014Article
- Genome wide analysis of the complete GlnR nitrogen-response regulon in Mycobacterium smegmatis.BMC genomics · 2013Article
- Adenylylation of mycobacterial Glnk (PII) protein is induced by nitrogen limitation.Tuberculosis (Edinburgh, Scotland) · 2013Article
- The role of glutamine oxoglutarate aminotransferase and glutamate dehydrogenase in nitrogen metabolism in Mycobacterium bovis BCG.PloS one · 2013Article
- Methionine sulfoximine resistance in Mycobacterium tuberculosis is due to a single nucleotide deletion resulting in increased expression of the major glutamine synthetase, GlnA1.Microbial drug resistance (Larchmont, N.Y.) · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Glutamine synthetase (GS) plays an important role in nitrogen assimilation. The major GS of Mycobacterium tuberculosis is GlnA1, a type I GS whose activity is controlled by posttranscriptional modification by GlnE. GlnE is an adenylyl transferase comprised of an adenylylating domain and a deadenylylating domain which modulate GS activity. We previously demonstrated that GlnE is essential in M. tuberculosis in normal growth medium. In this study, we further show that GlnE is required under multiple medium conditions, including in nitrogen-limited medium. We demonstrate that adenylylation is the critical activity for M. tuberculosis survival, since we were able to delete the deadenylylation domain with no apparent effect on growth or GS activity. Furthermore, we identified a critical aspartate residue in the proposed nucleotidyltransferase motif. Temperature-sensitive mutants of GlnE were generated and shown to have a defect in growth and GS activity in nitrogen-limited medium. Finally, we were able to generate a GlnE null mutant in the presence of L-methionine sulfoximine, a GS inhibitor, and glutamine supplementation. In the presence of these supplements, the null mutant was able to grow similarly to the wild type. Surprisingly, the GlnE mutant was able to survive and grow for extended periods in liquid medium, but not on solid medium, in the absence of GS inhibition. Thus, we have confirmed that the unusual requirement of M. tuberculosis for GlnE adenylylation activity is linked to the activity of GS in the cell.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.