The Phage Shock Protein Response

Flores-Kim, Josué; Darwin, Andrew J.

doi:10.1146/annurev-micro-102215-095359

Cited by 105 publications

(117 citation statements)

References 108 publications

(207 reference statements)

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“…The envelope also houses danger-sensing systems, such as dedicated two-component systems and accessory sigma factors that activate global adaptive response pathways (for examples, [1–4]). One mechanism for maintaining envelope integrity is the phage shock protein (Psp) response, a multi-gene system involving a cascade of protein interactions that stabilize the cell membrane during times of stress [5–7]. …”

Section: Prelude: Mechanisms For Preserving Cell Envelope Homeostasismentioning

confidence: 99%

Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme

Manganelli

Gennaro

2017

Trends in Microbiology

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During envelope stress, critical inner-membrane functions are preserved by the phage-shock-protein (Psp) system, a stress response that emerged from work with Escherichia coli and other Gram-negative bacteria. Reciprocal regulatory interactions and multiple effector functions are well documented in these organisms. Searches for the Psp system across phyla reveals conservation of only one protein, PspA. However, examination of Firmicutes and Actinobacteria reveals that PspA orthologs associate with non-orthologous regulatory and effector proteins retaining functions similar to those in Gram-negative counterparts. Conservation across phyla emphasizes the long-standing importance of the Psp system in prokaryotes, while inter- and intra-phyla variations within the system indicate adaptation to different cell envelope structures, bacterial lifestyles, and/or bacterial morphogenetic strategies.

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Section: Prelude: Mechanisms For Preserving Cell Envelope Homeostasismentioning

confidence: 99%

Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme

Manganelli

Gennaro

2017

Trends in Microbiology

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“…Moreover, since cell shape results from the reciprocal influence of mechanical forces and chemical interactions [64,65], the abovementioned link between PspA binding to the membrane and mechanical properties of the membrane [32] further suggests that Psp function, maintenance of membrane integrity, and the bacterial rod-like shape may be connected. Finally, we note that the cytoskeletal, actinlike proteins of E. coli, B. subtilis, and Actinobacteria differ from each other [66,67], This figure highlights interactions and functional parallels among orthologous and nonorthologous proteins in the three Psp systems rather than mechanistic/localization properties that are reviewed elsewhere [7]. Each factor in the system is indicated by a box.…”

Section: Outstanding Questionsmentioning

confidence: 77%

“…In the absence of stress, PspA binds to PspF and prevents PspF interaction with RpoN. During stress, recruitment of PspA to the cell membrane by PspB/PspC results in release of PspF from PspA-mediated inhibition, PspF interaction with RpoN, and induction of the Psp response (reviewed in [5][6][7]). …”

Section: Box 1 Transcriptional Regulation Of Known Psp Systemsmentioning

confidence: 99%

“…Neither dissipation of proton motive force nor redox state of the quinone pool have proven to be convincing candidates (reviewed in [7]). It was recently proposed, as is the case for other Manganelli peripheral membrane proteins [31], that a feedback mechanism exists between biophysical properties of the membrane, such as stored curvature elastic (SCE) stress, and PspA [32].…”

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confidence: 99%

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Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme

Manganelli¹,

Gennaro²

2017

Trends in Microbiology

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During envelope stress, critical inner-membrane functions are preserved by the phage-shockprotein (Psp) system, a stress response that emerged from work with Escherichia coli and other Gram-negative bacteria. Reciprocal regulatory interactions and multiple effector functions are well documented in these organisms. Searches for the Psp system across phyla reveals conservation of only one protein, PspA. However, examination of Firmicutes and Actinobacteria reveals that PspA orthologs associate with non-orthologous regulatory and effector proteins retaining functions similar to those in Gram-negative counterparts. Conservation across phyla emphasizes the longstanding importance of the Psp system in prokaryotes, while inter-and intra-phyla variations within the system indicate adaptation to different cell envelope structures, bacterial lifestyles, and/or bacterial morphogenetic strategies.

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“…There are a small number of additional genes in the Psp regulons of these two species, but pspF, pspA, pspB, and pspC are considered to encode the core components because only they are essential for regulation and/or stress tolerance (5,6,16,17). PspF is a DNA-binding protein that activates pspA operon expression in response to conditions that might adversely affect the inner membrane (18,19).…”

Section: Importancementioning

confidence: 99%

Interactions between the Cytoplasmic Domains of PspB and PspC Silence the Yersinia enterocolitica Phage Shock Protein Response

Flores-Kim

Darwin

2016

J Bacteriol

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The phage shock protein (Psp) system is a widely conserved cell envelope stress response that is essential for the virulence of some bacteria, including Yersinia enterocolitica. Recruitment of PspA by the inner membrane PspB-PspC complex characterizes the activated state of this response. The PspB-PspC complex has been proposed to be a stress-responsive switch, changing from an OFF to an ON state in response to an inducing stimulus. NT in vivo. These findings have provided the first insight into the regulatory function of the N-terminal cytoplasmic domain of PspC, revealing that its ability to participate in an inhibitory complex is essential to silencing the Psp response. IMPORTANCEThe phage shock protein (Psp) response has generated widespread interest because it is linked to important phenotypes, including antibiotic resistance, biofilm formation, and virulence in a diverse group of bacteria. Therefore, achieving a comprehensive understanding of how this response is controlled at the molecular level has obvious significance. An integral inner membrane protein complex is believed to be a critical regulatory component that acts as a stress-responsive switch, but some essential characteristics of the switch states are poorly understood. This study provides an important advance by uncovering a new protein interaction domain within this membrane protein complex that is essential to silencing the Psp response in the absence of an inducing stimulus. E xtracytoplasmic stress responses (ESRs) are a widely used strategy to protect bacterial cell envelopes from conditions and external agents that could compromise them. They monitor features within the cell envelope and direct a transcriptional response to potentially deleterious changes (1-4). One widely conserved ESR is the phage shock protein (Psp) response, which protects the cytoplasmic membrane from events that could increase its permeability (recently reviewed in references 5 and 6). Although it was discovered and initially studied in Escherichia coli (7), the Psp response is conserved in many Gram-negative bacteria, including the human pathogens Yersinia enterocolitica and Salmonella enterica serovar Typhimurium, where it is essential for virulence (8-11). Sequence and/or functional homologues of some Psp components also occur in Gram-positive bacteria, mycobacteria, archaea, and plant chloroplasts (e.g., references 1, 12, and 13). Furthermore, in addition to virulence, the Psp response has been linked to other important processes in bacteria, including the formation of biofilms and antibiotic-tolerant persister cells (14,15).Most research to date has focused on the Psp responses of E. coli and Y. enterocolitica, in which the core components are encoded by pspF and the adjacent divergently transcribed pspABC genes. There are a small number of additional genes in the Psp regulons of these two species, but pspF, pspA, pspB, and pspC are considered to encode the core components because only they are essential for regulation and/or stress tolerance (5,6,16,17...

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The Phage Shock Protein Response

Cited by 105 publications

References 108 publications

Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme

Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme

Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme

Interactions between the Cytoplasmic Domains of PspB and PspC Silence the Yersinia enterocolitica Phage Shock Protein Response

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