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Escherichia coli
About: Escherichia coli is a research topic. Over the lifetime, 59041 publications have been published within this topic receiving 2050337 citations. The topic is also known as: E. coli & E coli jdj.
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TL;DR: While significant differences were found between the two organisms in the effect of specific RBS elements on translation, other mRNA components in addition to those elements tested appear to be responsible, in part, for translational species specificity.
Abstract: A method is described to determine simultaneously the effect of any changes in the ribosome-binding site (RBS) of mRNA on translational efficiency in Bacillus subtilis and Escherichia coli in vivo. The approach was used to analyse systematically the influence of spacing between the Shine-Dalgarno sequence and the initiation codon, the three different initiation codons, and RBS secondary structure on translational yields in the two organisms. Both B. subtilis and E. coli exhibited similar spacing optima of 7-9 nucleotides. However, B. subtilis translated messages with spacings shorter than optimal much less efficiently than E. coli. In both organisms, AUG was the preferred initiation codon by two- to threefold. In E. coli GUG was slightly better than UUG while in B. subtilis UUG was better than GUG. The degree of emphasis placed on initiation codon type, as measured by translational yield, was dependent on the strength of the Shine-Dalgarno interaction in both organisms. B. subtilis was also much less able to tolerate secondary structure in the RBS than E. coli. While significant differences were found between the two organisms in the effect of specific RBS elements on translation, other mRNA components in addition to those elements tested appear to be responsible, in part, for translational species specificity. The approach described provides a rapid and systematic means of elucidating such additional determinants.
319 citations
TL;DR: It is shown that a histone-like bacterial protein has an important role in this novel example of thermoregulation of transcription of digalactoside-specific binding by uropathogenic strains of Escherichia coli 1.
Abstract: Expression of specific adhesive properties by bacteria in general seems to be regulated to fit the environmental conditions. An example is the transcriptional regulation of digalactoside-specific binding by uropathogenic strains of Escherichia coli. The fimbrial structures (pili) on the bacterial surface carry the adhesin and are present during growth at 37 degrees C but are not produced by cells at lower temperatures, such as 25 degrees C. Thermoregulation of expression is due to temperature-dependent transcription of a regulatory cistron in the pilus-adhesin gene cluster. We have now identified and characterized a new regulatory locus (drdX) and show that a histone-like bacterial protein has an important role in this novel example of thermoregulation of transcription.
319 citations
TL;DR: A comparison between the amino acid sequences of LT-B and CT-B is reported to show significant amino acid sequence homology, and several features of the eltB cistron were revealed by the sequence analysis.
Abstract: Cholera toxin (CT) and the Escherichia coli heat-labile toxin (LT) are functionally, structurally and immunologically similar enterotoxins. Both toxins cause the elevation of cyclic AMP levels in gut epithelial cells1,2 by catalysing the NAD-dependent ADP ribosylation of membrane proteins3–6. Each toxin is composed of two dissimilar subunits7,8. The A subunit has an enzymatic activity and is the adenylate cyclase-activating component of the enterotoxin4–11. The B subunit recognizes membrane components and binds the holotoxin to the target cell juxtaposing the A subunit with its substrates9,12. Binding studies and competition experiments indicate that the membrane receptors for cholera toxin B subunit (CT-B) and LT-B are similar but not identical13 (these studies were performed before LT was purified to homogeneity). The monosialosylganglioside GMI has been shown to be the receptor for the cholera toxin14, and it probably composes part of the receptor for LT. Gyles and Barnum15 first reported that LT and cholera toxin were immunologically related, and it has subsequently been shown that they share common antigenic determinants in both A and B subunits16. The primary structure of CT-B has been determined17,18. We report here a comparison between the amino acid sequences of LT-B and CT-B. The nucleotide sequence of the LT-B cistron (eltB) was determined using a recombinant plasmid encoding LT9. Translation of this sequence revealed that LT-B and CT-B show significant amino acid sequence homology. In addition, several features of the eltB cistron were revealed by the sequence analysis.
319 citations
TL;DR: This compound was purified from E. coli ΔlytB mutants by preparative anion exchange chromatography, and identified by mass spectrometry, 1H, 13C and 31P NMR spectroscopy, and NOESY analysis as (E)‐4‐hydroxy‐3‐methyl‐but‐2‐enyl pyrophosphate (HMB‐PP).
319 citations
TL;DR: Results suggest that NEIL2 is involved in global genome repair mainly for removing oxidative products of cytosine, which is similar to NEIL1 in having N-terminal Pro as the active site.
317 citations