Model Uracil-Rich RNAs and Membrane Protein mRNAs Interact Specifically with Cold Shock Proteins in Escherichia coli

Benhalevy, Daniel; Bochkareva, Elena; Biran, Ido; Bibi, Eitan

doi:10.1371/journal.pone.0134413

Cited by 18 publications

(30 citation statements)

References 46 publications

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“…These proteins are further controlled by heat shock factors, which are mainly altered under stress conditions 34 . In E. coli 381, the enhanced expression of acid shock protein (asr) 73 , acid resistance proteins hdeA, hdeB, and hdeD 12 , heat shock proteins IbpA, IbpB, Hsp31, and HspQ 15 , 74 , and cold shock protein cspA 75 , 76 reflected the genetic potential for survival of the pathogen in a diversified and harsh environment. Most enteric bacteria like E. coli contain acid-shock resistant proteins.…”

Section: Discussionmentioning

confidence: 99%

Virulence and transcriptome profile of multidrug-resistant Escherichia coli from chicken

Hussain

Zahid

Seleem

et al. 2017

Sci Rep

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Numerous studies have examined the prevalence of pathogenic Escherichia coli in poultry and poultry products; however, limited data are available regarding their resistance- and virulence-associated gene expression profiles. This study was designed to examine the resistance and virulence of poultry E. coli strains in vitro and in vivo via antibiotic susceptibility, biofilm formation and adhesion, and invasion and intracellular survivability assays in Caco-2 and Raw 264.7 cell lines as well as the determination of the median lethal dose in two-day old chickens. A clinical pathogenic multidrug-resistant isolate, E. coli 381, isolated from broilers, was found to be highly virulent in cell culture and 1000-fold more virulent in a chicken model than other strains; accordingly, the isolate was subsequently selected for transcriptome analysis. The comparative gene expression profile of MDR E. coli 381 and the reference human strain E. coli ATCC 25922 was completed with Illumina HiSeq. 2500 transcriptome analysis. Differential gene expression analysis indicates that there are multiple pathways involved in the resistance and virulence of this highly virulent strain. The results garnered from this study provide critical information about the highly virulent MDR E. coli strain of poultry origin and warrant further investigation due to its significant threat to public health.

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Section: Discussionmentioning

confidence: 99%

Virulence and transcriptome profile of multidrug-resistant Escherichia coli from chicken

Hussain

Zahid

Seleem

et al. 2017

Sci Rep

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“…The results of these experiments showed no preference for MPRs or CPRs in how they were influenced by FtsY-depletion, suggesting that the effect is indirect, probably through the role of FtsY in membrane protein biogenesis. While searching for factors that may have a direct role in the biogenesis of MPRs specifically, we have recently discovered that cold shock proteins (CSPs) such as CspE specifically interact with MPRs in vitro and in vivo [ 15 ]. Therefore, the role of CspE in the subcellular distribution of MPRs was examined next.…”

Section: Resultsmentioning

confidence: 99%

“…coli , and possibly also elsewhere, might be selectively recognized through features derived from their high uracil content in long segments throughout their coding sequence (~60 nucleotide-long) [ 14 ]. To investigate this hypothesis, we previously searched for uracil-rich RNA-binding proteins [ 15 ]. These studies led to the identification a highly specific interaction that takes place between transcripts that mimic MPRs and the cold shock proteins CspE and CspC, which are normally expressed under physiological conditions.…”

Section: Introductionmentioning

confidence: 99%

“…These studies led to the identification a highly specific interaction that takes place between transcripts that mimic MPRs and the cold shock proteins CspE and CspC, which are normally expressed under physiological conditions. The specific interaction with CspE occurred in vivo not only with the model uracil-rich transcripts but also with endogenous MPRs [ 15 ]. Here, towards better understanding of the biogenesis of MPRs and their interactions with cold shock proteins, we utilized biochemical fractionation to investigate the subcellular distribution of mRNAs in Escherichia coli with emphasis on MPRs and the role of CspE.…”

Section: Introductionmentioning

confidence: 99%

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Evidence for a cytoplasmic pool of ribosome-free mRNAs encoding inner membrane proteins in Escherichia coli

et al. 2017

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Translation-independent mRNA localization represents an emerging concept in cell biology. In Escherichia coli, mRNAs encoding integral membrane proteins (MPRs) are targeted to the membrane where they are translated by membrane associated ribosomes and the produced proteins are inserted into the membrane co-translationally. In order to better understand aspects of the biogenesis and localization of MPRs, we investigated their subcellular distribution using cell fractionation, RNA-seq and qPCR. The results show that MPRs are overrepresented in the membrane fraction, as expected, and depletion of the signal recognition particle-receptor, FtsY reduced the amounts of all mRNAs on the membrane. Surprisingly, however, MPRs were also found relatively abundant in the soluble ribosome-free fraction and their amount in this fraction is increased upon overexpression of CspE, which was recently shown to interact with MPRs. CspE also conferred a positive effect on the membrane-expression of integral membrane proteins. We discuss the possibility that the effects of CspE overexpression may link the intriguing subcellular localization of MPRs to the cytosolic ribosome-free fraction with their translation into membrane proteins and that the ribosome-free pool of MPRs may represent a stage during their targeting to the membrane, which precedes translation.

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“…Recently, two cold-shock proteins, CspE and CspC, were shown to interact with uracil-rich transcripts and the inner membrane of E . coli [56]. This suggests that these CSPs not only stabilize transcripts during cold shock, but also deliver specific U-rich cargos to the cytoplasmic membrane.…”

Section: Discussionmentioning

confidence: 99%

On the Spatial Organization of mRNA, Plasmids, and Ribosomes in a Bacterial Host Overexpressing Membrane Proteins

et al. 2016

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By using fluorescence imaging, we provide a time-resolved single-cell view on coupled defects in transcription, translation, and growth during expression of heterologous membrane proteins in Lactococcus lactis. Transcripts encoding poorly produced membrane proteins accumulate in mRNA-dense bodies at the cell poles, whereas transcripts of a well-expressed homologous membrane protein show membrane-proximal localization in a translation-dependent fashion. The presence of the aberrant polar mRNA foci correlates with cessation of cell division, which is restored once these bodies are cleared. In addition, activation of the heat-shock response and a loss of nucleoid-occluded ribosomes are observed. We show that the presence of a native-like N-terminal domain is key to SRP-dependent membrane localization and successful production of membrane proteins. The work presented gives new insights and detailed understanding of aberrant membrane protein biogenesis, which can be used for strategies to optimize membrane protein production.

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Model Uracil-Rich RNAs and Membrane Protein mRNAs Interact Specifically with Cold Shock Proteins in Escherichia coli

Cited by 18 publications

References 46 publications

Virulence and transcriptome profile of multidrug-resistant Escherichia coli from chicken

Virulence and transcriptome profile of multidrug-resistant Escherichia coli from chicken

Evidence for a cytoplasmic pool of ribosome-free mRNAs encoding inner membrane proteins in Escherichia coli

On the Spatial Organization of mRNA, Plasmids, and Ribosomes in a Bacterial Host Overexpressing Membrane Proteins

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