Escherichia coli K-12
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA171495 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Purpose: We use the ribosome profiling protocol to understand why EF4 confers resistance to tellurite and how tellurite affects ribosome. Methods: We used ribosome profiling and transcriptomic data to analyze mainly by plastid software. The ribosome were purified by sucrose gradient separation. Results: Using polysome profile and sequencing data, we found that tellurite disables the ribosome subunits to form a functional 70S ribosome and reduces the ribosome density after tellurite exposure. We also found that tellurite influences the ribosome reaching to stop codon. Tellurite shortened the ribosome protected fragment, this process was mediated by EF4. EF4 mediated more gene expression including these known tellurite resistance genes to confer tellurite resistance. Tellurite also induced many differential gene expression. Conclusions: Tellurite exerts its toxicity on ribosome by disabling 70S ribosome formation, reaching to stop codon, and inducing differential gene expression.
2021-01-29 | GSE109907 | GEO
Project description:Transcriptional profiling comparing Escherichia coli simultaneously exposed to tellurite and CTX with untreated control cells; Tellurite with control; CTX with control Three-condition experiment, antibacterial (tellurite; CTX or tellurite/CTX) vs. Untreated control cells. Biological replicates: 3 control, 3 toxicants exposed cells, independently grown and harvested. One replicate per array.
2013-09-01 | E-GEOD-39696 | biostudies-arrayexpress
Project description:Transcriptional profiling comparing Escherichia coli simultaneously exposed to tellurite and CTX with untreated control cells; Tellurite with control; CTX with control
2013-09-01 | GSE39696 | GEO
Project description:Horizontal gene transfer (HGT) is the major mechanism responsible for spread of antibiotic resistance. Antibiotic treatment has been suggested to promote HGT, either by directly affecting the conjugation process itself or by selecting for conjugations subsequent to DNA transfer. However, recent research suggests that the effect of antibiotic treatment on plasmid conjugation frequencies, and hence the spread of resistance plasmids, may have been overestimated. We addressed the question by quantifying transfer proteins and conjugation frequencies of a blaCTX-M-1 encoding IncI1 resistance plasmid in Escherichia coli MG1655 in the presence and absence of therapeutically relevant concentrations of cefotaxime (CTX). Analysis of the proteome by iTRAQ labeling and liquid chromatography tandem mass spectrometry revealed that Tra proteins were significantly up regulated in the presence of CTX. The up-regulation of the transfer machinery was confirmed at the transcriptional level for five selected genes. The CTX treatment did not cause induction of the SOS39 response as revealed by absence of significantly regulated SOS associated proteins in the proteome and no significant up-regulation of recA and sfiA genes. The frequency of plasmid conjugation, measured in an antibiotic free environment, increased significantly when the donor was pre-grown in broth containing CTX compared to growth without this drug, regardless of whether blaCTX-M-1 was located on the plasmid or in trans on the chromosome. The results shows that antibiotic treatment can affect expression of a plasmid conjugation machinery and subsequent DNA transfer.
2017-11-21 | PXD006679 | Pride
Project description:Transcriptional profiling of E. coli cultures exposed to tellurite 0.5 µg/ml
| PRJNA251514 | ENA
Project description:Increased virulence mediated by subinhibitory concentrations of Cefotaxime (CTX)
| PRJNA264057 | ENA
Project description:Escherichia coli (E. coli) amine oxidase (ECAO) encoded by tynA gene has been one of the model enzymes to study the mechanism of oxidative deamination of amines to the corresponding aldehydes by amine oxidases. The biological roles of ECAO have been less addressed. Therefore we have constructed a gene deletion Escherichia coli K-12 strain, E. coli tynA-, and used the microarray technique to address its function by comparing the total RNA gene expression to the one of the wt. Our results suggest that tynA is a reserve gene for stringent environmental conditions and its gene product ECAO a growth advantage compared to other bacteria due to H2O2 production.
2015-09-30 | GSE65385 | GEO
Project description:Escherichia coli mutation accumulation experimental evolution mediated by DnaK
| PRJNA320472 | ENA
Project description:Analysis of tellurite resistance gene, tehA, in Shiga toxin-producing Escherichia coli O157
| PRJDB17012 | ENA
Project description:The flavodoxins are flavin mononucleotide-containing electron transferases. Flavodoxin I has been presumed to be the only flavodoxin of Escherichia coli, and its gene, fldA, is known to belong to the soxRS (superoxide response) oxidative stress regulon. An insertion mutation of fldA was constructed and was lethal under both aerobic and anaerobic conditions; only cells that also had an intact (fldA(+)) allele could carry it. A second flavodoxin, flavodoxin II, was postulated, based on the sequence of its gene, fldB. Unlike the fldA mutant, an fldB insertion mutant is a viable prototroph in the presence or absence of oxygen. A high-copy-number fldB(+) plasmid did not complement the fldA mutation. Therefore, there must be a vital function for which FldB cannot substitute for flavodoxin I. An fldB-lacZ fusion was not induced by H(2)O(2) and is therefore not a member of the oxyR regulon. However, it displayed a soxS-dependent induction by paraquat (methyl viologen), and the fldB gene is preceded by two overlapping regions that resemble known soxS binding sites. The fldB insertion mutant did not have an increased sensitivity to the effects of paraquat on either cellular viability or the expression of a soxS-lacZ fusion. Therefore, fldB is a new member of the soxRS (superoxide response) regulon, a group of genes that is induced primarily by univalent oxidants and redox cycling compounds. However, the reactions in which flavodoxin II participates and its role during oxidative stress are unknown.
| S-EPMC101859 | biostudies-literature