Recent structural advances in bacterial chemotaxis signalling

Riechmann, Carlos; Zhang, Peijun

doi:10.1016/j.sbi.2023.102565

Cited by 2 publications

(3 citation statements)

References 49 publications

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“…Intriguingly, part of the ZorA tail (residues 540-729) shows homology with the core signaling unit of the bacterial chemosensory array ( Extended Data Fig. 3b ), which contains a long intracellular helical bundle responsible for transferring signal from the extracellular environment into the cell and regulates the activities of the subsequent effectors 23 . Sequence analyses further reveal that the length of the tail appears consistent across Zorya subtypes, suggesting that a uniform tail length is functionally essential ( Extended Data Fig.…”

Section: Resultsmentioning

confidence: 99%

“…12a, b ). A somewhat similar sensory transmission mechanism occurs with bacterial chemosensory arrays and the long ZorA tail might serve to transmit the signal in a manner analogous to the long coiled-coil cytoplasmic signaling domains of methyl-accepting chemotaxis proteins 23 . A second hypothesis that would explain the need for both rotation and a long ZorA tail is that rotation might allow the ‘reeling in’ of the phage DNA around the tail ( Extended Data Fig.…”

Section: Discussionmentioning

confidence: 97%

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Structure and mechanism of Zorya anti-phage defense system

Hu,

Hughes,

Popp

et al. 2023

Preprint

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SummaryZorya is a recently identified and widely distributed bacterial immune system, which protects against phage invasion. It consists of a predicted membrane-embedded complex (ZorAB) and soluble components that differ among Zorya subtypes, notably ZorC and ZorD, in type I Zorya systems. Here, we reveal the molecular basis of the Zorya defense system using cryo-electron microscopy, mutagenesis, fluorescence microscopy, proteomics, and functional studies. We demonstrate that ZorAB shares the stoichiometry of other 5:2 inner membrane ion-driven rotary motors. Additionally, ZorA5B2features a dimeric ZorB peptidoglycan binding domain and a pentameric α-helical coiled-coil tail made of ZorA that projects approximately 700 Å into the cytoplasm. We further characterize the structure and function of the soluble Zorya components, ZorC and ZorD, and find that they harbour DNA binding and nuclease activity, respectively. Comprehensive functional and mutational analyses demonstrates that all Zorya components work in concert to protect bacterial cells against invading phages. We present evidence that ZorAB operates as an ion-driven motor that becomes activated and anchors to the cell wall upon sensing of cell envelope perturbations during phage invasion. Subsequently, ZorAB transfers the phage invasion signal through the ZorA cytoplasmic tail to the soluble effectors, which function to prevent phage propagation. In summary, our study elucidates the foundational mechanisms of Zorya function and reveals a novel triggering signal for the rapid activation of an anti-phage defense system.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 97%

Structure and mechanism of Zorya anti-phage defense system

Hu,

Hughes,

Popp

et al. 2023

Preprint

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“…The components and signal transduction mechanisms of chemotaxis networks are highly conserved among chemotactic bacteria ( Wuichet and Zhulin, 2010 ). Chemoreceptors (also termed methyl-accepting chemotaxis proteins or transducer-like proteins [Tlps]) typically oligomerize into trimers of dimers, to form repetitive hexagonal arrays, sense stimuli, and transmit signals to regulate the activity of the histidine kinase CheA ( Hazelbauer et al, 2008 ; Briegel et al, 2012 ; Riechmann and Zhang, 2023 ). The response regulator CheY accepts a phosphoryl group from the activated CheA, while the phosphorylated CheY interacts with the flagellar motor(s), thereby changing the direction of flagellar rotation and allowing bacteria to swim towards attractants or away from repellents ( Bi and Sourjik, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

Identification of a dCache-type chemoreceptor in Campylobacter jejuni that specifically mediates chemotaxis towards methyl pyruvate

Zhao,

Yao,

et al. 2024

Front. Microbiol.

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The foodborne pathogenic bacterium Campylobacter jejuni utilizes chemotaxis to assist in the colonization of host niches. A key to revealing the relationship among chemotaxis and pathogenicity is the discovery of signaling molecules perceived by the chemoreceptors. The C. jejuni chemoreceptor Tlp11 is encoded by the highly infective C. jejuni strains. In the present study, we report that the dCache-type ligand-binding domain (LBD) of C. jejuni ATCC 33560 Tlp11 binds directly to novel ligands methyl pyruvate, toluene, and quinoline using the same pocket. Methyl pyruvate elicits a strong chemoattractant response, while toluene and quinoline function as the antagonists without triggering chemotaxis. The sensory LBD was used to control heterologous proteins by constructing chimeras, indicating that the signal induced by methyl pyruvate is transmitted across the membrane. In addition, bioinformatics and experiments revealed that the dCache domains with methyl pyruvate-binding sites and ability are widely distributed in the order Campylobacterales. This is the first report to identify the class of dCache chemoreceptors that bind to attractant methyl pyruvate and antagonists toluene and quinoline. Our research provides a foundation for understanding the chemotaxis and virulence of C. jejuni and lays a basis for the control of this foodborne pathogen.

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Recent structural advances in bacterial chemotaxis signalling

Cited by 2 publications

References 49 publications

Structure and mechanism of Zorya anti-phage defense system

Structure and mechanism of Zorya anti-phage defense system

Identification of a dCache-type chemoreceptor in Campylobacter jejuni that specifically mediates chemotaxis towards methyl pyruvate

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