Heat shock proteins IbpA and IbpB are required for NlpI-participated cell division in Escherichia coli

Tao, Jing; Sang, Yu; Teng, Qihui; Ni, Jinjing; Yang, Kevin Yi; Tsui, Stephen Kwok‐Wing; Yao, Yufeng

doi:10.3389/fmicb.2015.00051

Cited by 14 publications

(12 citation statements)

References 50 publications

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“…This approach was chosen to minimize the changes in the secondary structure of the mRNA, as ibpA and ibpB genes are arranged in a single operon and transcribed into polycistronic mRNA. However, as reported previously [39], nonsense mutations in either ibpA or ibpB resulted in the increase in the cellular level of the remaining sHsp expressed at heat shock conditions as compared to the wild type strain (Fig 9A).…”

Section: Resultssupporting

confidence: 84%

Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates

et al. 2019

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Small heat shock proteins (sHsps) are a conserved class of ATP-independent chaperones that bind to aggregation-prone polypeptides at stress conditions. sHsps encage these polypeptides in assemblies, shielding them from further aggregation. To facilitate their subsequent solubilization and refolding by Hsp70 (DnaK) and Hsp100 (ClpB) chaperones, first, sHsps need to dissociate from the assemblies. In most γ-proteobacteria, these functions are fulfilled by a single sHsp (IbpA), but in a subset of Enterobacterales, a two-protein sHsp (IbpA and IbpB) system has evolved. To gain insight into the emergence of complexity within this chaperone system, we reconstructed the phylogeny of γ-proteobacteria and their sHsps. We selected proteins representative of systems comprising either one or two sHsps and analysed their ability to form sHsps-substrate assemblies. All the tested IbpA proteins, but not IbpBs, stably interact with an aggregating substrate. Moreover, in Escherichia coli cells, ibpA but not ibpB suppress the growth defect associated with low DnaK level, which points to the major protective role of IbpA during the breakdown of protein quality control. We also examined how sHsps affect the association of Hsp70 with the assemblies at the initial phase of disaggregation and how they affect protein recovery after stress. Our results suggest that a single gene duplication event has given rise to the sHsp system consisting of a strong canonical binder, IbpA, and its non-canonical paralog IbpB that enhances sHsps dissociation from the assemblies. The cooperation between the sHsps reduces the demand for Hsp70 needed to outcompete them from the assemblies by promoting sHsps dissociation without compromising assembly formation at heat shock. This potentially increases the robustness and elasticity of sHsps protection against irreversible aggregation.

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Section: Resultssupporting

confidence: 84%

Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates

et al. 2019

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“…The protein-protein interaction between PhoP and Pat or CobB were detected by Bacterial Two-Hybrid System (Stratagene) according to the previous procedure [ 57 ]. The phoP and pat or cobB genes were cloned into pBT and pTRG, respectively.…”

Section: Methodsmentioning

confidence: 99%

Acetylation of Lysine 201 Inhibits the DNA-Binding Ability of PhoP to Regulate Salmonella Virulence

et al. 2016

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The two-component system PhoP-PhoQ is highly conserved in bacteria and regulates virulence in response to various signals for bacteria within the mammalian host. Here, we demonstrate that PhoP could be acetylated by Pat and deacetylated by deacetylase CobB enzymatically in vitro and in vivo in Salmonella Typhimurium. Specifically, the conserved lysine residue 201(K201) in winged helix–turn–helix motif at C-terminal DNA-binding domain of PhoP could be acetylated, and its acetylation level decreases dramatically when bacteria encounter low magnesium, acid stress or phagocytosis of macrophages. PhoP has a decreased acetylation and increased DNA-binding ability in the deletion mutant of pat. However, acetylation of K201 does not counteract PhoP phosphorylation, which is essential for PhoP activity. In addition, acetylation of K201 (mimicked by glutamine substitute) in S. Typhimurium causes significantly attenuated intestinal inflammation as well as systemic infection in mouse model, suggesting that deacetylation of PhoP K201 is essential for Salmonella pathogenesis. Therefore, we propose that the reversible acetylation of PhoP K201 may ensure Salmonella promptly respond to different stresses in host cells. These findings suggest that reversible lysine acetylation in the DNA-binding domain, as a novel regulatory mechanism of gene expression, is involved in bacterial virulence across microorganisms.

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“…Finally, the high levels of inflammation characterizing IBD likely affect the microbiota as they do the host, inducing molecular and physiological changes. It was found that in response to harsh environments E. coli —which is found enriched in IBD patients (Table 1 )—could up-regulate the ibpA and ibpB genes belonging to the stress response regulon, which are involved in cell division, signal transduction and intestinal adhesion (Zuckert, 2014 ; Tao et al, 2015 ). In the IL10 −/− IBD model mouse inoculated with a murine isolate of colitis-inducing E. coli (NC101), ibpA and ibpB were found to be activated, presumably to cope with the high amounts of reactive oxygen species induced by intestinal inflammation and—possibly—by the increased temperature caused by inflammation (Patwa et al, 2011 ).…”

Section: Pathologies With Altered Gi Microbiomementioning

confidence: 99%

Human Gut Microbiota: Toward an Ecology of Disease

et al. 2017

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Composed of trillions of individual microbes, the human gut microbiota has adapted to the uniquely diverse environments found in the human intestine. Quickly responding to the variances in the ingested food, the microbiota interacts with the host via reciprocal biochemical signaling to coordinate the exchange of nutrients and proper immune function. Host and microbiota function as a unit which guards its balance against invasion by potential pathogens and which undergoes natural selection. Disturbance of the microbiota composition, or dysbiosis, is often associated with human disease, indicating that, while there seems to be no unique optimal composition of the gut microbiota, a balanced community is crucial for human health. Emerging knowledge of the ecology of the microbiota-host synergy will have an impact on how we implement antibiotic treatment in therapeutics and prophylaxis and how we will consider alternative strategies of global remodeling of the microbiota such as fecal transplants. Here we examine the microbiota-human host relationship from the perspective of the microbial community dynamics.

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Heat shock proteins IbpA and IbpB are required for NlpI-participated cell division in Escherichia coli

Cited by 14 publications

References 50 publications

Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates

Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates

Acetylation of Lysine 201 Inhibits the DNA-Binding Ability of PhoP to Regulate Salmonella Virulence

Human Gut Microbiota: Toward an Ecology of Disease

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