New Roles for HAMP Domains: the Tri-HAMP Region of Pseudomonas aeruginosa Aer2 Controls Receptor Signaling and Cellular Localization

Anaya, Selina; Orillard, Emilie; Greer‐Phillips, Suzanne E.; Watts, Kylie J.

doi:10.1128/jb.00225-22

Cited by 4 publications

(7 citation statements)

References 51 publications

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“…PA0075 ( pppA ) is predicted to encode a regulatory component of the type VI secretion system (T6SS) in P. aeruginosa ( 35 ). PA0176 (aer2) is predicted to encode a methyl-accepting chemotaxis protein (Aer2), which senses oxygen and mediates stress responses, virulence and chemotaxis behaviour ( 36 ). PA5017 ( dipA ) is predicted to encode the phosphodiesterase DipA that contributes to biofilm dispersion by modulating c-di-GMP and polysaccharide levels ( 37 ).…”

Section: Resultsmentioning

confidence: 99%

Adaptation ofPseudomonas aeruginosato repeated invasion into a commensal competitor

Wheatley,

Shaw,

Shah

et al. 2024

Preprint

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The host-associated microbiome is an important barrier to bacterial pathogen colonization and can mediate protection through a variety of mechanisms. We wanted to investigate the potential consequences of selection imposed by commensal bacterial competitors on an invading bacterial pathogen. To do this, we tested the ability of the opportunistic pathogenPseudomonas aeruginosato invade pre-established communities of an abundant commensal bacterium in the human microbiome,Staphylococcus epidermidis. We passaged ten independent lines ofP. aeruginosathrough daily invasion into a pre-establishedS. epidermidispopulation (coculture evolved lines), alongside daily passage through monoculture conditions (monoculture evolved lines). The monoculture evolved lines showed strong parallel evolution in the Wsp (Wrinkly spreader phenotype) signal transducing system involved in biofilm formation, and significantly elevated biofilm formation. On the other hand, adaptation toS. epidermidisoccurred via mutations in a diverse set of genes, and the coculture evolved lines showed much weaker evidence for parallel evolution, suggesting that the selective pressure imposed by competition withS. epidermidisis more complex than the pressure imposed by culture conditions. Interestingly, the elevated biofilm formation phenotype seen in the monoculture evolved lines was not observed in the lines evolved in the presence ofS. epidermidis, raising the question of whether enhanced biofilm formation did not evolve withS. epidermidispresent because it was not beneficial, or becauseS. epidermidismay be able to restrict this evolutionary path by inhibiting biofilm formation.

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Section: Resultsmentioning

confidence: 99%

Adaptation ofPseudomonas aeruginosato repeated invasion into a commensal competitor

Wheatley,

Shaw,

Shah

et al. 2024

Preprint

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“…Removing tri‐HAMP alters the PAS dimer interface and causes the distal PAS interface to splay apart. This abolishes signaling, even in the presence of PAS signal‐on lesions (Anaya et al, 2022 ; Orillard et al, 2021 ). Thus, unlike Pa Aer2 and Vc Aer2, Vv Aer2 and Li Aer2 can apparently maintain a physiologically‐appropriate PAS dimer interface in the absence of any N‐terminal domains.…”

Section: Discussionmentioning

confidence: 99%

“…The domains N‐terminal to the Aer2 core vary between bacterial genera and within species, and serve different roles. The tri‐HAMP region at the N‐terminus of Pa Aer2 functions as a moveable scaffold to correctly orient and poise PAS dimers for O 2 ‐mediated signaling (Anaya et al, 2022 ). In contrast, the additional PAS domain at the N‐terminus of Vc Aer2 ( Vc PAS1) serves as a signal modulator (Greer‐Phillips et al, 2018 ), similar to Vv PAS2 in this study.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to these roles, PAS domains are also known to function as signal transducers, dimerization or interaction motifs, and protein localization determinants (Stuffle et al, 2021 ). The HAMP1 domain of Pa Aer2 was recently shown to be a protein clustering and localization determinant (Anaya et al, 2022 ). Such a role for the PAS1 domains of Vc Aer2 and Vv Aer2 is conceivable given that Aer2 receptors form membrane‐associated polar clusters (Ortega et al, 2020 ).…”

Section: Discussionmentioning

confidence: 99%

“… Structural models of four different Aer2 receptors highlighting the conserved Aer2 core, different numbers of PAS‐heme domains and distinctive N‐terminal domain arrangements. Alphafold2 dimer models from left to right: P. aeruginosa Aer2 [ Pa Aer2, model from (Anaya et al, 2022 )], V. cholerae Aer2 ( Vc Aer2, this study), V. vulnificus Aer2 ( Vv Aer2, this study), and L. interrogans Aer2 [ Li Aer2, model from (Orillard & Watts, 2022 )]. The Aer core comprises an O 2 ‐sensing PAS‐heme domain connected to C‐terminal di‐HAMP and kinase control domains.…”

Section: Discussionmentioning

confidence: 99%

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The Aer2 chemoreceptor from Vibrio vulnificus is a tri‐PAS‐heme oxygen sensor

Stuffle

Suzuki

Orillard

et al. 2022

Molecular Microbiology

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The marine pathogen Vibrio vulnificus senses and responds to environmental stimuli via two chemosensory systems and 42–53 chemoreceptors. Here, we present an analysis of the V. vulnificus Aer2 chemoreceptor, VvAer2, which is the first V. vulnificus chemoreceptor to be characterized. VvAer2 is related to the Aer2 receptors of other gammaproteobacteria, but uncharacteristically contains three PAS domains (PAS1‐3), rather than one or two. Using an E. coli chemotaxis hijack assay, we determined that VvAer2, like other Aer2 receptors, senses and responds to O2. All three VvAer2 PAS domains bound pentacoordinate b‐type heme and exhibited similar O2 affinities. PAS2 and PAS3 both stabilized O2 via conserved Iβ‐Trp residues, but PAS1, which was easily oxidized in vitro, was unaffected by Iβ‐Trp replacement. Our results support a model in which PAS1 is largely dispensable for O2‐mediated signaling, whereas PAS2 modulates PAS3 signaling, and PAS3 signals to the downstream domains. Each PAS domain appeared to be positionally optimized, because PAS swapping caused altered signaling properties, and neither PAS1 nor PAS2 could replace PAS3. Our findings strengthen previous conclusions that Aer2 receptors are O2 sensors, but with distinct N‐terminal domain arrangements that facilitate, modulate and tune responses based on environmental signals.

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Control of bacterial second messenger signaling and motility by heme-based direct oxygen-sensing proteins

Hoque,

Weinert

2023

Current Opinion in Microbiology

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New Roles for HAMP Domains: the Tri-HAMP Region of Pseudomonas aeruginosa Aer2 Controls Receptor Signaling and Cellular Localization

Cited by 4 publications

References 51 publications

Adaptation ofPseudomonas aeruginosato repeated invasion into a commensal competitor

Adaptation ofPseudomonas aeruginosato repeated invasion into a commensal competitor

The Aer2 chemoreceptor from Vibrio vulnificus is a tri‐PAS‐heme oxygen sensor

Control of bacterial second messenger signaling and motility by heme-based direct oxygen-sensing proteins

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