A proteomic study of Corynebacterium glutamicumAAA+ protease FtsH

Lüdke, Alja; Krämer, Reinhard; Burkovski, Andreas; Schluesener, Daniela; Poetsch, Ansgar

doi:10.1186/1471-2180-7-6

Cited by 22 publications

(13 citation statements)

References 38 publications

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“… reported 37‐fold increase in the bacterial protein “ascorbate‐specific IIB component” of Salmonella infantis when internalized into lettuce leaf in comparison to those grown in the LB medium. Similarly, 50‐fold increase in biotin carboxylase/biotin carboxyl carrier protein (accBC) has been reported in ftsH‐deleted mutant of Corynebacterium glutamicum in comparison to the wild variety .…”

Section: Discussionmentioning

confidence: 66%

“…In the present study, about 60‐ and 40‐fold increase in protein abundance for SOD and ferritin, respectively, was observed in the heat‐exposed group, which appears to be quite high. However, such high values in protein abundance have been reported earlier . Wang et al.…”

Section: Discussionmentioning

confidence: 73%

“…In the present study, about 60-and 40-fold increase in protein abundance for SOD and ferritin, respectively, was observed in the heat-exposed group, which appears to be quite high. However, such high values in protein abundance have been reported earlier [28][29][30]. Wang et al observed 40-fold increase in dihydroxynaphthoic acid synthetase and 3533-fold decrease in transaldolase in halophilic Salinicoccus roseus in response to lactate stress [28].…”

Section: Discussionmentioning

confidence: 90%

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Proteomic changes in the liver of Channa striatus in response to high temperature stress

et al. 2016

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The present study was undertaken to investigate the proteomic changes in the liver of murrel Channa striatus exposed to high temperature stress. Fishes were exposed to 36°C for 4 days and liver proteome changes were analyzed using gel- based proteomics, i.e. 2DE, MALDI-TOF/TOF-MS, and validation by transcript analysis. The study showed, besides others, increased abundance of two sets of proteins, the antioxidative enzymes superoxide dismutase (SOD), ferritin, cellular retinol binding protein (CRBP), glutathione-S-transferase (GST), and the chaperones HSP60 and protein disulfide isomerase; this was validated by transcript analysis. The proteome data are available via ProteomeXchange with identifier PXD002608. Further, gene expression analysis was also carried out in the fishes exposed to thermal stress for longer durations (30 days experimental exposure in laboratory and for 30 days beyond, taking Channa collected from a hot spring runoff at 36-38°C); sod, gst, crbp, and hsp60 were found to continue to remain upregulated at eight-, 2.5-, 2.4-, and 2.45-fold, respectively, in the hot spring runoff fish. Pathway analysis showed that the upregulations of the antioxidant enzymes as well as molecular chaperones are induced by the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2). Thus, while short-term heat stress tolerance involves the antioxidative enzymes SOD, ferritin, CRBP, GST, and chaperones HSP60 and protein disulfide isomerase, adaptation under chronic heat stress is associated with SOD, CRBP, GST, and HSP60.

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Section: Discussionmentioning

confidence: 66%

Section: Discussionmentioning

confidence: 73%

Section: Discussionmentioning

confidence: 90%

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Proteomic changes in the liver of Channa striatus in response to high temperature stress

et al. 2016

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“…In E. coli and Bacillus subtilis, FtsH is induced by heat and osmotic shocks (43,44). While FtsH is not essential for growth in species such as B. subtilis, Corynebacterium glutamicum, and Lactobacillus plantarum (44)(45)(46), FtsH is essential for some bacteria, including E. coli and Lactococcus lactis (47,48). Our repeated attempts to inactivate ftsH in S. mutans were unsuccessful, suggesting that FtsH is also essential in this organism.…”

Section: Discussionmentioning

confidence: 99%

ClpL Is Required for Folding of CtsR in Streptococcus mutans

Tao¹,

Biswas²

2012

Journal of Bacteriology

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ClpL, a member of the HSP100 family, is widely distributed in Gram-positive bacteria but is absent in Gram-negative bacteria. Although ClpL is involved in various cellular processes, such as the stress tolerance response, long-term survival, virulence, and antibiotic resistance, the detailed molecular mechanisms are largely unclear. Here we report that ClpL acts as a chaperone to properly fold CtsR, a stress response repressor, and prevents it from forming protein aggregates in Streptococcus mutans. In vitro, ClpL was able to successfully refold urea-denatured CtsR but not aggregated proteins. We suggest that ClpL recognizes primarily soluble but denatured substrates and prevents the formation of large protein aggregates. We also found that in vivo, the C-terminal D2-small domain of ClpL is essential for the observed chaperone activity. Since ClpL widely contributes to various cellular functions, we speculate that ClpL chaperone activity is necessary to maintain cellular homeostasis.

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“…The E proteolysis pathway (19) and Cpx two-component signal transduction system (20) are involved in envelope maintenance, adaptation, and protection in response to environmental stress (21)(22)(23)(24)(25). Both pathways regulate the expression and constitutive degradation of misfolded proteins within the cell periplasm.…”

mentioning

confidence: 99%

Precipitation of Iron on the Surface of Leptospira interrogans Is Associated with Mutation of the Stress Response Metalloprotease HtpX

Henry

Khoo

et al. 2013

Appl Environ Microbiol

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e High concentrations of free metal ions in the environment can be detrimental to bacterial survival. However, bacteria utilize strategies, including the activation of stress response pathways and immobilizing chemical elements on their surface, to limit this toxicity. In this study, we characterized LA4131, the HtpX-like M48 metalloprotease from Leptospira interrogans, with a putative role in bacterial stress response and membrane homeostasis. Growth of the la4131 transposon mutant strain (L522) in 360 M FeSO 4 (10-fold the normal in vitro concentration) resulted in the production of an amorphous iron precipitate. Atomic force microscopy and transmission electron microscopy analysis of the strain demonstrated that precipitate production was associated with the generation and release of outer membrane vesicles (OMVs) from the leptospiral surface. Transcriptional studies indicated that inactivation of la4131 resulted in altered expression of a subset of metal toxicity and stress response genes. Combining these findings, this report describes OMV production in response to environmental stressors and associates OMV production with the in vitro activity of an HtpX-like metalloprotease.

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A proteomic study of Corynebacterium glutamicumAAA+ protease FtsH

Cited by 22 publications

References 38 publications

Proteomic changes in the liver of Channa striatus in response to high temperature stress

Proteomic changes in the liver of Channa striatus in response to high temperature stress

ClpL Is Required for Folding of CtsR in Streptococcus mutans

Precipitation of Iron on the Surface of Leptospira interrogans Is Associated with Mutation of the Stress Response Metalloprotease HtpX

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