Lactococcus lactis ZitR Is a Zinc-Responsive Repressor Active in the Presence of Low, Nontoxic Zinc Concentrations In Vivo

Llull, Daniel; Son, Olivier; Blanié, Sandrine; Briffotaux, Julien; Morello, Eric; Rogniaux, Hélène; Danot, Olivier; Poquet, Isabelle

doi:10.1128/jb.01109-10

Cited by 25 publications

(44 citation statements)

References 55 publications

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“…MarR proteins that respond to salicylate, urate, zinc, and a number of antibiotics have been studied (1,21,27,42). Also, MarR regulators for aromatic catabolic pathways that respond to m-chlorobenzoate, m-hydroxybenzoate, and p-hydroxybenzoate have been reported (5,32,45).…”

Section: Discussionmentioning

confidence: 99%

Anaerobic p -Coumarate Degradation by Rhodopseudomonas palustris and Identification of CouR, a MarR Repressor Protein That Binds p -Coumaroyl Coenzyme A

et al. 2012

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The phenylpropanoid p-coumarate and structurally related aromatic compounds are produced in large amounts by green plants and are excellent carbon sources for many soil bacteria. Aerobic bacteria remove the acyl side chain from phenylpropanoids to leave an aromatic aldehyde, which then enters one of several possible central pathways of benzene ring degradation. We investigated the pathway for the anaerobic degradation of p-coumarate by the phototrophic bacterium Rhodopseudomonas palustris and found that it also follows this metabolic logic. We characterized enzymes for the conversion of p-coumarate to p-hydroxybenzaldehyde and acetyl coenzyme A (acetyl-CoA) encoded by the couAB operon. We also identified a MarR family transcriptional regulator that we named CouR. A couR mutant had elevated couAB expression. In addition, His-tagged CouR bound with high affinity to a DNA fragment encompassing the couAB promoter region, and binding was abrogated by the addition of nanomolar quantities of p-coumaroyl-CoA but not by p-coumarate. Footprinting demonstrated binding of CouR to an inverted repeat sequence that overlaps the ؊10 region of the couAB promoter. Our results provide evidence for binding of a CoA-modified aromatic compound by a MarR family member. Although the MarR family is widely distributed in bacteria and archaea and includes over 12,000 members, ligands have been identified for relatively few family members. Here we provide biochemical evidence for a new category of MarR ligand.

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Section: Discussionmentioning

confidence: 99%

Anaerobic p -Coumarate Degradation by Rhodopseudomonas palustris and Identification of CouR, a MarR Repressor Protein That Binds p -Coumaroyl Coenzyme A

et al. 2012

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“…Purified ZitR is a dimer with up to two zinc ligands per monomer. It specifically binds two intact palindromic operator sites overlapping the Ϫ35 and Ϫ10 boxes of the zit promoter (75). ZitR requires Zn 2ϩ to bind DNA, and transcriptional analyses have shown that zitSQP expression is induced only at Zn 2ϩ concentrations below 100 nM, indicating that ZitR acts as a sensor of Zn 2ϩ scarcity (75).…”

Section: One-component Systemsmentioning

confidence: 99%

“…It specifically binds two intact palindromic operator sites overlapping the Ϫ35 and Ϫ10 boxes of the zit promoter (75). ZitR requires Zn 2ϩ to bind DNA, and transcriptional analyses have shown that zitSQP expression is induced only at Zn 2ϩ concentrations below 100 nM, indicating that ZitR acts as a sensor of Zn 2ϩ scarcity (75). S. pneumoniae encodes a homologous Zn 2ϩ uptake system (AdcABC) that is regulated by a ZitR homolog (AdcR) (76).…”

Section: One-component Systemsmentioning

confidence: 99%

Stress Physiology of Lactic Acid Bacteria

Papadimitriou

Alegría

Bron

et al. 2016

Microbiol Mol Biol Rev

515

404

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SUMMARYLactic acid bacteria (LAB) are important starter, commensal, or pathogenic microorganisms. The stress physiology of LAB has been studied in depth for over 2 decades, fueled mostly by the technological implications of LAB robustness in the food industry. Survival of probiotic LAB in the host and the potential relatedness of LAB virulence to their stress resilience have intensified interest in the field. Thus, a wealth of information concerning stress responses exists today for strains as diverse as starter (e.g.,Lactococcus lactis), probiotic (e.g., severalLactobacillusspp.), and pathogenic (e.g.,EnterococcusandStreptococcusspp.) LAB. Here we present the state of the art for LAB stress behavior. We describe the multitude of stresses that LAB are confronted with, and we present the experimental context used to study the stress responses of LAB, focusing on adaptation, habituation, and cross-protection as well as on self-induced multistress resistance in stationary phase, biofilms, and dormancy. We also consider stress responses at the population and single-cell levels. Subsequently, we concentrate on the stress defense mechanisms that have been reported to date, grouping them according to their direct participation in preserving cell energy, defending macromolecules, and protecting the cell envelope. Stress-induced responses of probiotic LAB and commensal/pathogenic LAB are highlighted separately due to the complexity of the peculiar multistress conditions to which these bacteria are subjected in their hosts. Induction of prophages under environmental stresses is then discussed. Finally, we present systems-based strategies to characterize the “stressome” of LAB and to engineer new food-related and probiotic LAB with improved stress tolerance.

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“…First, AdcR (ZitR in L. lactis 25 ) has a unique effector in Zn(II). Additionally, the co-repression mechanism induced by metal binding to AdcR is unprecedented in MarR family transcriptional regulators.…”

mentioning

confidence: 99%

Crystal Structure of the Zinc-Dependent MarR Family Transcriptional Regulator AdcR in the Zn(II)-Bound State

2011

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S. pneumoniae adhesin competence regulator (AdcR), the first metal dependent member of the MarR family of proteins, represses the transcription of a high affinity zinc-specific uptake transporter, a group of surface antigen zinc-binding pneumococcal histidine triad proteins (PhtA, PhtB, PhtD and PhtE) and an AdcA homologue (AdcAII). The 2.0 Å resolution structure of Zn(II)-bound AdcR reveals a highly helical two-fold symmetric dimer with two distinct metal binding sites per protomer. Zn(II) is tetrahedrally coordinated by E24, H42, H108 and H112 in what defines the primary sensing site in AdcR. Site 2 is a tetracoordinate site whose function is currently unknown. NMR methyl group perturbation experiments reveal that Zn(II) drives a global change in the structure of apo-AdcR that stabilizes an “open” conformation that is compatible with DNA binding. The structure also reveals a hydrogen-bonding network that is predicted to play a role in the allosteric coupling of Zn(II) binding to high affinity DNA binding in a co-repression mechanism that is unprecedented in MarR transcriptional regulators.

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Lactococcus lactis ZitR Is a Zinc-Responsive Repressor Active in the Presence of Low, Nontoxic Zinc Concentrations In Vivo

Cited by 25 publications

References 55 publications

Anaerobic p -Coumarate Degradation by Rhodopseudomonas palustris and Identification of CouR, a MarR Repressor Protein That Binds p -Coumaroyl Coenzyme A

Anaerobic p -Coumarate Degradation by Rhodopseudomonas palustris and Identification of CouR, a MarR Repressor Protein That Binds p -Coumaroyl Coenzyme A

Stress Physiology of Lactic Acid Bacteria

Crystal Structure of the Zinc-Dependent MarR Family Transcriptional Regulator AdcR in the Zn(II)-Bound State

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