Fine-tuning of amino sugar homeostasis by EIIANtr in Salmonella Typhimurium

Yoo, Woongjae; Yoon, Hyunjin; Seok, Yeong‐Jae; Lee, Chang-Ro; Lee, Hyung Ho; Ryu, Sangryeol

doi:10.1038/srep33055

Cited by 27 publications

(39 citation statements)

References 61 publications

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“…Intracellular balance between nitrogen and carbon was found to modulate the phosphorylation status of EIIA Ntr , the output regulator of PTS Ntr 36. In addition, the availability of amino sugar was recently revealed to control the degradation rate of EIIA Ntr 37. The finding that the positive role of EIIA Ntr in pdu or prp expression is remarkable only in the presence of 1,2-PDL or propionate prompted analysis of whether the expression or activity of EIIA Ntr could be enhanced in response to 1,2-PDL or propionate.…”

Section: Resultsmentioning

confidence: 99%

Enzyme IIANtr Regulates Salmonella Invasion Via 1,2-Propanediol And Propionate Catabolism

Yoo

Kim

Yoon

et al. 2017

Sci Rep

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Many Proteobacteria possess a nitrogen-metabolic phosphotransferase system (PTSNtr) consisting of EINtr, NPr, and EIIANtr (encoded by ptsP, ptsO, and ptsN, respectively). The PTSNtr plays diverse regulatory roles, but the substrate phosphorylated by EIIANtr and its primary functions have not yet been identified. To comprehensively understand the roles of PTSNtr in Salmonella Typhimurium, we compared the whole transcriptomes of wild-type and a ΔptsN mutant. Genome-wide RNA sequencing revealed that 3.5% of the annotated genes were up- or down-regulated by three-fold or more in the absence of EIIANtr. The ΔptsN mutant significantly down-regulated the expression of genes involved in vitamin B12 synthesis, 1,2-propanediol utilization, and propionate catabolism. Moreover, the invasiveness of the ΔptsN mutant increased about 5-fold when 1,2-propanediol or propionate was added, which was attributable to the increased stability of HilD, the transcriptional regulator of Salmonella pathogenicity island-1. Interestingly, an abundance of 1,2-propanediol or propionate promoted the production of EIIANtr, suggesting the possibility of a positive feedback loop between EIIANtr and two catabolic pathways. These results demonstrate that EIIANtr is a key factor for the utilization of 1,2-propanediol and propionate as carbon and energy sources, and thereby modulates the invasiveness of Salmonella via 1,2-propanediol or propionate catabolism.

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Section: Resultsmentioning

confidence: 99%

Enzyme IIANtr Regulates Salmonella Invasion Via 1,2-Propanediol And Propionate Catabolism

Yoo

Kim

Yoon

et al. 2017

Sci Rep

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“…On one hand, phosphorylation decreases the affinity of PtsN for KdpD ninefold. On the other hand, phosphorylated PtsN was recently shown to be engaged in interaction with the GlmS protein (Yoo et al ., ). The sequestration by GlmS, together with the reduced interaction potential (Fig.…”

Section: Discussionmentioning

confidence: 97%

Non‐canonical activation of histidine kinase KdpD by phosphotransferase protein PtsN through interaction with the transmitter domain

Mörk-Mörkenstein

Heermann

Göpel

et al. 2017

Molecular Microbiology

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The two-component system KdpD/KdpE governs K homeostasis by controlling synthesis of the high affinity K transporter KdpFABC. When sensing low environmental K concentrations, the dimeric kinase KdpD autophosphorylates in trans and transfers the phosphoryl-group to the response regulator KdpE, which subsequently activates kdpFABC transcription. In Escherichia coli, KdpD can also be activated by interaction with the non-phosphorylated form of the accessory protein PtsN. PtsN stimulates KdpD kinase activity thereby increasing phospho-KdpE levels. Here, we analyzed the interplay between KdpD/KdpE and PtsN. PtsN binds specifically to the catalytic DHp domain of KdpD, which is also contacted by KdpE. Accordingly, PtsN and KdpE compete for binding, providing a paradox. Low levels of non-phosphorylated PtsN stimulate, whereas high amounts reduce kdpFABC expression by blocking access of KdpE to KdpD. Ligand fishing experiments provided insight as they revealed ternary complex formation of PtsN/KdpD /KdpE in vivo demonstrating that PtsN and KdpE bind different protomers in the KdpD dimer. PtsN may bind one protomer to stimulate phosphorylation of the second KdpD protomer, which then phosphorylates bound KdpE. Phosphorylation of PtsN prevents its incorporation in ternary complexes. Interaction with the conserved DHp domain enables PtsN to regulate additional kinases such as PhoR.

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“…This could help to overcome envelope stress caused by precursor depletion. Recently, GlmS in Salmonella was reported to be inhibited by protein PtsN in response to glutamine and GlcN6P levels (Yoo et al , ). How GlcN6P is sensed by PtsN is unknown, but our work uncovers RapZ as feasible candidate.…”

Section: Discussionmentioning

confidence: 99%

Small RNA ‐binding protein RapZ mediates cell envelope precursor sensing and signaling in Escherichia coli

et al. 2020

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The RNA‐binding protein RapZ cooperates with small RNAs (sRNAs) GlmY and GlmZ to regulate the glmS mRNA in Escherichia coli. Enzyme GlmS synthesizes glucosamine‐6‐phosphate (GlcN6P), initiating cell envelope biosynthesis. GlmZ activates glmS expression by base‐pairing. When GlcN6P is ample, GlmZ is bound by RapZ and degraded through ribonuclease recruitment. Upon GlcN6P depletion, the decoy sRNA GlmY accumulates through a previously unknown mechanism and sequesters RapZ, suppressing GlmZ decay. This circuit ensures GlcN6P homeostasis and thereby envelope integrity. In this work, we identify RapZ as GlcN6P receptor. GlcN6P‐free RapZ stimulates phosphorylation of the two‐component system QseE/QseF by interaction, which in turn activates glmY expression. Elevated GlmY levels sequester RapZ into stable complexes, which prevents GlmZ decay, promoting glmS expression. Binding of GlmY also prevents RapZ from activating QseE/QseF, generating a negative feedback loop limiting the response. When GlcN6P is replenished, GlmY is released from RapZ and rapidly degraded. We reveal a multifunctional sRNA‐binding protein that dynamically engages into higher‐order complexes for metabolite signaling.

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Fine-tuning of amino sugar homeostasis by EIIANtr in Salmonella Typhimurium

Cited by 27 publications

References 61 publications

Enzyme IIANtr Regulates Salmonella Invasion Via 1,2-Propanediol And Propionate Catabolism

Enzyme IIANtr Regulates Salmonella Invasion Via 1,2-Propanediol And Propionate Catabolism

Non‐canonical activation of histidine kinase KdpD by phosphotransferase protein PtsN through interaction with the transmitter domain

Small RNA ‐binding protein RapZ mediates cell envelope precursor sensing and signaling in Escherichia coli

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