The multicopy sRNA LhrC controls expression of the oligopeptide-binding protein OppA in<i>Listeria monocytogenes</i>

Sievers, Susanne; Lund, Anja; Menendez-Gil, Pilar; Nielsen, Aaraby Yoheswaran; Mollerup, Maria Storm; Nielsen, Stine Lambert; Larsson, Pernille Buch; Borch-Jensen, Jonas; Johansson, Jörgen; Kallipolitis, Birgitte H.

doi:10.1080/15476286.2015.1071011

Cited by 41 publications

(71 citation statements)

References 56 publications

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“…3C]) and the subtilisin-like protease (SCLAV_p0750), which were expressed at some sampling times at levels 10.1-and 6.4-fold higher than those in the wild-type strain, respectively (Table 1). Coregulated expression of independent substrate-binding proteins and secreted proteins has been described previously (23).…”

Section: Resultsmentioning

confidence: 99%

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Transcriptional Studies on a Streptomyces clavuligerus oppA2 Deletion Mutant: N -Acetylglycyl-Clavaminic Acid Is an Intermediate of Clavulanic Acid Biosynthesis

Álvarez-Álvarez

Rodrı́guez-Garcı́a

Martínez-Burgo

et al. 2018

Appl Environ Microbiol

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The gene encodes an oligopeptide-binding protein similar to the periplasmic substrate-binding proteins of the ABC transport systems. However, is an orphan gene, not included in an ABC operon. This gene is located in the clavulanic acid (CA) gene cluster of and is essential for CA production. A transcriptomic study of the-null mutant Δ:: showed changes in the expression levels of 233 genes from those in the parental strain. These include genes for ABC transport systems, secreted proteins, peptidases, and proteases. Expression of the clavulanic acid, clavam, and cephamycin C biosynthesis gene clusters was not significantly affected in the deletion mutant. The genes for holomycin biosynthesis were upregulated 2-fold on average, and the level of upregulation increased to 43-fold in a double mutant lacking and the pSCL4 plasmid. Strains in which was mutated secreted into the culture the compound-acetylglycyl-clavaminic acid (AGCA), a putative intermediate of CA biosynthesis. A culture broth containing AGCA, or AGCA purified by liquid chromatography-mass spectrometry (LC-MS), was added to the cultures of various non-CA-producing mutants. Mutants blocked in the early steps of the pathway restored CA production, whereas mutants altered in late steps did not, establishing that AGCA is a late intermediate of the biosynthetic pathway, which is released from the cells when the oligopeptide-binding protein OppA2 is not available. The gene encodes an oligopeptide permease essential for the production of clavulanic acid. A transcriptomic analysis of Δ:: in comparison to the parental strain ATCC 27064 is reported. The lack of OppA2 results in different expression of 233 genes, including genes for proteases and genes for transport systems. The expression of the clavulanic acid genes in the mutant is not significantly affected, but the genes for holomycin biosynthesis are strongly upregulated, in agreement with the higher holomycin production by this strain. The -mutant is known to release-acetylglycyl-clavaminic acid to the broth. Cosynthesis assays using non-clavulanic acid-producing mutants showed that the addition of pure -acetylglycyl-clavaminic acid to mutants in which clavulanic acid formation was blocked resulted in the recovery of clavulanic acid production, but only in mutants blocked in the early steps of the pathway. This suggests that-acetylglycyl-clavaminic acid is a previously unknown late intermediate of the clavulanic acid pathway.

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Section: Resultsmentioning

confidence: 99%

“…OppA periplasmic proteins are important in chemotaxis and virulence due to their substrate-binding and transport abilities as part of ABC systems (23,28). In addition, ecto-ATPase activity (29) or chaperone-like functions in protein folding (30) have been described for these proteins.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional Studies on a Streptomyces clavuligerus oppA2 Deletion Mutant: N -Acetylglycyl-Clavaminic Acid Is an Intermediate of Clavulanic Acid Biosynthesis

Álvarez-Álvarez

Rodrı́guez-Garcı́a

Martínez-Burgo

et al. 2018

Appl Environ Microbiol

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“…Additional studies in L. monocytogenes showed that the Hfqbinding sRNA LhrC also acts by direct base pairing to the RBS of partner mRNAs, but no role for Hfq has been found so far in controlling the stability or regulatory activities of LhrC [8,[11][12][13]. LhrC is a multicopy sRNA and the LhrC family comprises seven siblings: LhrC1-5, Rli22 and Rli33-1 (reviewed in [5]).…”

Section: Introductionmentioning

confidence: 99%

“…For LhrC1-5 and Rli22, induction relies on the twocomponent system LisRK, whereas the general stress sigma factor SigmaB controls expression of Rli33-1 [11,13]. The LhrC family of sRNAs has been shown to target mRNAs encoding surfaceexposed virulence-associated proteins, including the virulence adhesin LapB, the oligo-peptide binding protein OppA, and the CD4 + T cell-stimulating antigen TcsA [11,12]. In all three cases, the sRNAs exert a negative effect on translation, and for lapB and oppA, the LhrCs are known to act by direct base pairing to the RBS, leading to inhibition of translation followed by mRNA degradation [11,12].…”

Section: Introductionmentioning

confidence: 99%

“…The LhrC family of sRNAs has been shown to target mRNAs encoding surfaceexposed virulence-associated proteins, including the virulence adhesin LapB, the oligo-peptide binding protein OppA, and the CD4 + T cell-stimulating antigen TcsA [11,12]. In all three cases, the sRNAs exert a negative effect on translation, and for lapB and oppA, the LhrCs are known to act by direct base pairing to the RBS, leading to inhibition of translation followed by mRNA degradation [11,12]. For tcsA, however, LhrC-meditated control appears not to follow the canonical pathway.…”

Section: Introductionmentioning

confidence: 99%

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The LhrC sRNAs control expression of T cell-stimulating antigen TcsA in Listeria monocytogenes by decreasing tcsA mRNA stability

et al. 2019

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The bacterial pathogen Listeria monocytogenes encodes seven homologous small regulatory RNAs, named the LhrC family of sRNAs. The LhrCs are highly induced under infection-relevant conditions and are known to inhibit the expression of multiple target mRNAs encoding virulence-associated surface proteins. In all cases studied so far, the LhrCs use their CU-rich regions for base pairing to complementary AG-rich sequences of the ribosomal binding site (RBS) of specific target mRNAs. Consequently, LhrC-mRNA interaction results in inhibition of translation followed by mRNA degradation, corresponding to the canonical model for sRNA-mediated gene regulation in bacteria. Here, we demonstrate that the LhrC sRNAs employ a different regulatory mechanism when acting to down-regulate the expression of tcsA, encoding a T cell-stimulating antigen. In this case, LhrC base pairs to an AG-rich site located well upstream of the RBS in tcsA mRNA. Using an in vitro translation assay, we found that LhrC could not prevent the ribosome from translating the tcsA messenger. Rather, the LhrC sRNAs act to decrease the half-life of tcsA mRNA in vivo. Importantly, LhrC-mediated destabilization of tcsA mRNA relies on an intact LhrC binding site near the 5´-end of the tcsA mRNA and occurs independently of translation. Based on these findings, we propose an alternative mechanism for LhrC-mediated control in L. monocytogenes that relies solely on sRNA-induced degradation of a target mRNA.

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The role of RNA regulators, quorum sensing and c‐di‐GMP in bacterial biofilm formation

et al. 2022

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Biofilms provide an ecological advantage against many environmental stressors, such as pH and temperature, making it the most common life‐cycle stage for many bacteria. These protective characteristics make eradication of bacterial biofilms challenging. This is especially true in the health sector where biofilm formation on hospital or patient equipment, such as respirators, or catheters, can quickly become a source of anti‐microbial resistant strains. Biofilms are complex structures encased in a self‐produced polymeric matrix containing numerous components such as polysaccharides, proteins, signalling molecules, extracellular DNA and extracellular RNA. Biofilm formation is tightly controlled by several regulators, including quorum sensing (QS), cyclic diguanylate (c‐di‐GMP) and small non‐coding RNAs (sRNAs). These three regulators in particular are fundamental in all stages of biofilm formation; in addition, their pathways overlap, and the significance of their role is strain‐dependent. Currently, ribonucleases are also of interest for their potential role as biofilm regulators, and their relationships with QS, c‐di‐GMP and sRNAs have been investigated. This review article will focus on these four biofilm regulators (ribonucleases, QS, c‐di‐GMP and sRNAs) and the relationships between them.

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The multicopy sRNA LhrC controls expression of the oligopeptide-binding protein OppA inListeria monocytogenes

Cited by 41 publications

References 56 publications

Transcriptional Studies on a Streptomyces clavuligerus oppA2 Deletion Mutant: N -Acetylglycyl-Clavaminic Acid Is an Intermediate of Clavulanic Acid Biosynthesis

Transcriptional Studies on a Streptomyces clavuligerus oppA2 Deletion Mutant: N -Acetylglycyl-Clavaminic Acid Is an Intermediate of Clavulanic Acid Biosynthesis

The LhrC sRNAs control expression of T cell-stimulating antigen TcsA in Listeria monocytogenes by decreasing tcsA mRNA stability

The role of RNA regulators, quorum sensing and c‐di‐GMP in bacterial biofilm formation

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