ArticleProceedings of the National Academy of Sciences of the United States of America2012
Activation of Escherichia coli antiterminator BglG requires its phosphorylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Identification and regulation of an alternative PTS for disaccharide utilization inApplied and environmental microbiology · 2025Article
- In Vitro Antimicrobial Efficacy Assessment of Ethanolic, Aqueous, and Dual Solvent Extracts of MushroomAntibiotics (Basel, Switzerland) · 2024Article
- The effect of DNA-binding proteins on insertion sequence element transposition upstream of theFrontiers in microbiology · 2024Article
- An autoinhibitory mechanism controls RNA-binding activity of the nitrate-sensing protein NasR.Molecular microbiology · 2020Article
- Structural insight into glucose repression of the mannitol operon.Scientific reports · 2019Article
- Posttranscription Initiation Control of Gene Expression Mediated by Bacterial RNA-Binding Proteins.Annual review of microbiology · 2019Review
- Validation of Predicted Virulence Factors inToxins · 2019Article
- Regulation of Bacterial Gene Expression by Transcription Attenuation.Microbiology and molecular biology reviews : MMBR · 2019Review
- Diversity, versatility and complexity of bacterial gene regulation mechanisms: opportunities and drawbacks for applications in synthetic biology.FEMS microbiology reviews · 2019Review
- Interaction of lipoprotein QseG with sensor kinase QseE in the periplasm controls the phosphorylation state of the two-component system QseE/QseF in Escherichia coli.PLoS genetics · 2018Article
- Carbohydrate Utilization in Bacteria: Making the Most Out of Sugars with the Help of Small Regulatory RNAs.Microbiology spectrum · 2018Review
- Phosphotransferase-dependent accumulation of (p)ppGpp in response to glutamine deprivation in Caulobacter crescentus.Nature communications · 2016Article
- Phosphorylation events in the multiple gene regulator of group A Streptococcus significantly influence global gene expression and virulence.Infection and immunity · 2015Article
- Ascorbic acid-dependent gene expression in Streptococcus pneumoniae and the activator function of the transcriptional regulator UlaR2.Frontiers in microbiology · 2015Article
- In vitro transcriptome analysis of two Chinese isolates of Streptococcus suis serotype 2.Genomics, proteomics & bioinformatics · 2014Article
- The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.Microbiology and molecular biology reviews : MMBR · 2014Review
- Dynamic localization of a transcription factor in Bacillus subtilis: the LicT antiterminator relocalizes in response to inducer availability.Journal of bacteriology · 2013Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Transcriptional antiterminator proteins of the BglG family control the expression of enzyme II (EII) carbohydrate transporters of the bacterial phosphotransferase system (PTS). In the PTS, phosphoryl groups are transferred from phosphoenolpyruvate (PEP) via the phosphotransferases enzyme I (EI) and HPr to the EIIs, which phosphorylate their substrates during transport. Activity of the antiterminators is negatively controlled by reversible phosphorylation catalyzed by the cognate EIIs in response to substrate availability and positively controlled by the PTS. For the Escherichia coli BglG antiterminator, two different mechanisms for activation by the PTS were proposed. According to the first model, BglG is activated by HPr-catalyzed phosphorylation at a site distinct from the EII-dependent phosphorylation site. According to the second model, BglG is not activated by phosphorylation, but solely through interaction with EI and HPr, which are localized at the cell pole. Subsequently BglG is released from the cell pole to the cytoplasm as an active dimer. Here we addressed this discrepancy and found that activation of BglG requires phosphorylatable HPr or the HPr homolog FruB in vivo. Further, we uniquely demonstrate that purified BglG protein becomes phosphorylated by FruB as well as by HPr in vitro. Histidine residue 208 in BglG is essential for this phosphorylation. These data suggest that BglG is in fact activated by phosphorylation and that there is no principal difference between the PTS-exerted mechanisms controlling the activities of BglG family proteins in Gram-positive and Gram-negative bacteria.
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