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Phage shock protein pspa

Richard M Armstrong, Dominique C Carter, Samantha N Atkinson, Scott S Terhune, Thomas C Zahrt
Mycobacterium tuberculosis is a global pathogen of significant medical importance. A key aspect of its lifecycle is the ability to enter into an altered physiological state of non-replicating persistence during latency and resist elimination by the host immune system. One mechanism by which M. tuberculosis facilitates its survival during latency is by producing and metabolizing intracytoplasmic lipid droplets (LDs). LDs are semi-quasi organelles consisting of a neutral lipid core such as triacylglycerol surrounded by a phospholipid monolayer and proteins...
May 14, 2018: Journal of Bacteriology
Xiaowen Cui, Hsu-Ming Sherman Wen, Yoshimasa Kinoshita, Shota Koishi, Chika Isowaki, Liushu Ou, Yoshimitsu Masuda, Ken-Ichi Honjoh, Takahisa Miyamoto
 Sublethally heat-injured cells of Salmonella in food can recover under favorable conditions, leading to foodborne illness. To elucidate the molecular mechanism of recovery from heat injury, the global changes in gene transcription of Salmonella Typhimurium were investigated in previous study. In this study, the functions of genes involved in phage shock response (viz., phage shock protein (psp) genes), the transcription levels of which were found in previous study to be increased during recovery from heat injury, were investigated in recovering cells...
2018: Biocontrol Science
Janani Ravi, Vivek Anantharaman, L Aravind, Maria Laura Gennaro
The phage shock protein (Psp) stress-response system protects bacteria from envelope stress through a cascade of interactions with other proteins and membrane lipids to stabilize the cell membrane. A key component of this multi-gene system is PspA, an effector protein that is found in diverse bacterial phyla, archaea, cyanobacteria, and chloroplasts. Other members of the Psp system include the cognate partners of PspA that are part of known operons: pspF||pspABC in Proteobacteria, liaIHGFSR in Firmicutes, and clgRpspAMN in Actinobacteria...
May 2018: Antonie Van Leeuwenhoek
Riccardo Manganelli, Maria Laura Gennaro
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 reveal 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...
March 2017: Trends in Microbiology
Christopher McDonald, Goran Jovanovic, B A Wallace, Oscar Ces, Martin Buck
The phage shock protein (Psp) response maintains integrity of the inner membrane (IM) in response to extracytoplasmic stress conditions and is widely distributed amongst enterobacteria. Its central component PspA, a member of the IM30 peripheral membrane protein family, acts as a major effector of the system through its direct association with the IM. Under non-stress conditions PspA also negatively regulates its own expression via direct interaction with the AAA+ ATPase PspF. PspA has a counterpart in cyanobacteria called Vipp1, which is implicated in protection of the thylakoid membranes...
January 2017: Biochimica et Biophysica Acta
Josué Flores-Kim, Andrew J Darwin
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. In the OFF state, PspA cannot access its binding site in the C-terminal cytoplasmic domain of PspC (PspCCT ), because this site is bound to PspB...
December 15, 2016: Journal of Bacteriology
Richard M Armstrong, Katherine L Adams, Joseph E Zilisch, Daniel J Bretl, Hiromi Sato, David M Anderson, Thomas C Zahrt
UNLABELLED: Mycobacterium tuberculosis, the causative agent of tuberculosis (TB), remains a significant cause of morbidity and mortality worldwide, despite the availability of a live attenuated vaccine and anti-TB antibiotics. The vast majority of individuals infected with M. tuberculosis develop an asymptomatic latent infection in which the bacterium survives within host-generated granulomatous lesions in a physiologically altered metabolic state of nonreplicating persistence. The granuloma represents an adverse environment, as M...
June 1, 2016: Journal of Bacteriology
L Turkovicova, R Smidak, G Jung, J Turna, G Lubec, J Aradska
The tellurite resistance gene operon (ter) is widely spread among bacterial species, particularly pathogenic species. The ter operon has been implicated in tellurite resistance, phage inhibition, colicine resistance, and pathogenicity. The TerC protein represents one of the key proteins in tellurite resistance and shows no significant homology to any protein of known function. So far, there is no experimental evidence for TerC interaction partners. In this study, proteomic-based methods, including blue native electrophoresis and co-immunoprecipitation combined with LC-MS/MS, have been used to identify TerC interaction partners and thus providing indirect evidence for tentative functions of TerC in Escherichia coli...
March 16, 2016: Journal of Proteomics
Stephanie J Southern, Abigail Male, Timothy Milne, Mitali Sarkar-Tyson, Ali Tavassoli, Petra C F Oyston
The phage-shock protein (Psp) response is an extracytoplasmic response system that is vital for maintenance of the cytoplasmic membrane when the cell encounters stressful conditions. The paradigm of the Psp response has been established in Escherichia coli. The response has been shown to be important for survival during the stationary phase, maintenance of the proton motive force across membranes and implicated in virulence. In this study, we identified a putative PspA homologue in Burkholderia pseudomallei, annotated as BPSL2105...
November 2015: Microbiology
Christopher McDonald, Goran Jovanovic, Oscar Ces, Martin Buck
UNLABELLED: Phage shock protein A (PspA), which is responsible for maintaining inner membrane integrity under stress in enterobacteria, and vesicle-inducting protein in plastids 1 (Vipp1), which functions for membrane maintenance and thylakoid biogenesis in cyanobacteria and plants, are similar peripheral membrane-binding proteins. Their homologous N-terminal amphipathic helices are required for membrane binding; however, the membrane features recognized and required for expressing their functionalities have remained largely uncharacterized...
2015: MBio
Jin-Sook Kim, Min-Kyung Jeong, Bong-Seong Koo, Hyeon-Cheol Lee
A novel thymidine-producing strain of Escherichia coli was prepared by genome recombineering. Eleven genes were deleted by replacement with an expression cassette, and 7 genes were integrated into the genome. The resulting strain, E. coli HLT013, showed a high thymidine yield with a low deoxyuridine content. DNA microarrays were then used to compare the gene expression profiles of HLT013 and its isogenic parent strain. Based on microarray analysis, the pyr biosynthesis genes and 10 additional genes were selected and then expressed in HLT013 to find reasonable candidates for enhancing thymidine yield...
November 2015: Applied and Environmental Microbiology
Hendrik Osadnik, Michael Schöpfel, Eyleen Heidrich, Denise Mehner, Hauke Lilie, Christoph Parthier, H Jelger Risselada, Helmut Grubmüller, Milton T Stubbs, Thomas Brüser
Phage shock protein A (PspA) belongs to the highy conserved PspA/IM30 family and is a key component of the stress inducible Psp system in Escherichia coli. One of its central roles is the regulatory interaction with the transcriptional activator of this system, the σ(54) enhancer-binding protein PspF, a member of the AAA+ protein family. The PspA/F regulatory system has been intensively studied and serves as a paradigm for AAA+ enzyme regulation by trans-acting factors. However, the molecular mechanism of how exactly PspA controls the activity of PspF and hence σ(54) -dependent expression of the psp genes is still unclear...
November 2015: Molecular Microbiology
Parul Mehta, Goran Jovanovic, Liming Ying, Martin Buck
The bacterial cell envelope retains a highly dense cytoplasm. The properties of the cytoplasm change with the metabolic state of the cell, the logarithmic phase (log) being highly active and the stationary phase metabolically much slower. Under the differing growth phases, many different types of stress mechanisms are activated in order to maintain cellular integrity. One such response in enterobacteria is the phage shock protein (Psp) response that enables adaptation to the inner membrane (IM) stress. The Psp system consists of a transcriptional activator PspF, negative regulator PspA, signal sensors PspBC, with PspA and PspG acting as effectors...
April 2015: Biochemical Society Transactions
Josué Flores-Kim, Andrew J Darwin
The bacterial phage shock protein (Psp) system is a highly conserved cell envelope stress response required for virulence in Yersinia enterocolitica and Salmonella enterica. In non-inducing conditions the transcription factor PspF is inhibited by an interaction with PspA. In contrast, PspA associates with the cytoplasmic membrane proteins PspBC during inducing conditions. This has led to the proposal that PspBC exists in an OFF state, which cannot recruit PspA, or an ON state, which can. However, nothing was known about the difference between these two states...
May 1, 2015: Journal of Biological Chemistry
Lingang Zhang, Wataru Sakamoto
A protein designated as VIPP1 is found widely in organisms performing oxygenic photosynthesis, but its precise role in chloroplasts has remained somewhat mysterious. Based on its structural similarity, it presumably has evolved from bacterial Phage shock protein A (PspA) with a C-terminal extension of approximately 40 amino acids. Both VIPP1 and PspA are membrane-associated despite the lack of transmembrane helices. They form an extremely large homo-complex that consists of an oligomeric ring unit. Although PspA is known to respond to membrane stress and although it acts in maintaining proton motive force through membrane repair, the multiple function of VIPP1, such as vesicle budding from inner envelope to deliver lipids to thylakoids, maintenance of photosynthetic complexes in thylakoid membranes, biogenesis of Photosystem I, and protective role of inner envelope against osmotic stress, has been proposed...
September 2015: Biochimica et Biophysica Acta
W-C Tsai, T-Y Kuo, C-Y Lin, J-C Lin, W-J Chen
AIMS: To investigate whether Photobacterium damselae subsp. piscicida (Phdp) can sense and directly respond to the presence of cationic antimicrobial peptides (AMPs). METHODS AND RESULTS: We performed proteomic methodologies to investigate the responsive proteins of Phdp on exposure to AMP Q6. Proteins significantly altered were analysed by two-dimensional gel electrophoresis (2-DE) and LC-ESI-Q-TOF MS/MS, thus resulting in five outer membrane proteins (OMPs), seven inner membrane proteins (IMPs) and 17 cytoplasmic proteins (CPs) identified...
January 2015: Journal of Applied Microbiology
Inke Wallrodt, Lotte Jelsbak, Line E Thomsen, Lena Brix, Sébastien Lemire, Laurent Gautier, Dennis S Nielsen, Goran Jovanovic, Martin Buck, John E Olsen
The phage-shock protein (Psp) system is believed to manage membrane stress in all Enterobacteriaceae and has recently emerged as being important for virulence in several pathogenic species of this phylum. The core of the Psp system consists of the pspA-D operon and the distantly located pspG gene. In Salmonella enterica serovar Typhimurium (S. Typhimurium), it has recently been reported that PspA is essential for systemic infection of mice, but only in NRAMP1(+) mice, signifying that attenuation is related to coping with divalent cation starvation in the intracellular environment...
June 2014: Journal of Medical Microbiology
Goran Jovanovic, Parul Mehta, Christopher McDonald, Anthony C Davidson, Povilas Uzdavinys, Liming Ying, Martin Buck
The phage shock protein (Psp) systems found in bacteria, archaea and higher plants respond to extracytoplasmic stresses that damage the cytoplasmic membrane and enable cells to repair their membranes. The conserved membrane-associated effector protein PspA has four α-helical domains (HD1-HD4) and helps to repair the membrane as a high-order oligomer. In enterobacteria, under non-stress conditions, PspA as a low-order assembly directly inhibits its cognate transcription activator PspF. Here we show that N-terminal amphipathic helices ahA and ahB in PspA HD1 are functional determinants involved in negative gene control and stress signal perception and its transduction via interactions with the PspBC membrane stress sensors and the inner membrane (IM)...
April 3, 2014: Journal of Molecular Biology
Anthony W Kingston, Xiaojie Liao, John D Helmann
In Bacillus subtilis, the extracytoplasmic function (ECF) σ factors σ(M) , σ(W) and σ(X) all contribute to resistance against lantibiotics. Nisin, a model lantibiotic, has a dual mode of action: it inhibits cell wall synthesis by binding lipid II, and this complex also forms pores in the cytoplasmic membrane. These activities can be separated in a nisin hinge-region variant (N20P M21P) that binds lipid II, but no longer permeabilizes membranes. The major contribution of σ(M) to nisin resistance is expression of ltaSa, encoding a stress-activated lipoteichoic acid synthase, and σ(X) functions primarily by activation of the dlt operon controlling d-alanylation of teichoic acids...
November 2013: Molecular Microbiology
Nan Zhang, Timothy Simpson, Edward Lawton, Povilas Uzdavinys, Nicolas Joly, Patricia Burrows, Martin Buck
Bacterial enhancer binding proteins (bEBPs) are a subclass of the AAA(+) (ATPases Associated with various cellular Activities) protein family. They are responsible for σ(54)-dependent transcription activation during infection and function under many stressful growth conditions. The majority of bEBPs are regulated in their formation of ring-shaped hexameric self-assemblies via an amino-terminal domain through its phosphorylation or ligand binding. In contrast, the Escherichia coli phage shock protein F (PspF) is negatively regulated in trans by phage shock protein A (PspA)...
August 9, 2013: Journal of Molecular Biology
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