Transcriptional Response of<i>Escherichia coli</i>to External Zinc

Yamamoto, Kaneyoshi; Ishihama, Akira

doi:10.1128/jb.187.18.6333-6340.2005

Cited by 79 publications

(91 citation statements)

References 33 publications

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“…But, the level of htrA mRNA was significantly increased by copper in the cpxAR null mutant because htrAp is induced by sigma-E activation, as seen previously for zinc shock. 22) Transcripts from 11 promoters, cpxPp, ftnBp, htrAp, ppiAp, ybaJp1, yccAp, ydeHp, yihEp, yebEp, yobBp, and yqjAp, were detected without copper in the wild type, whereas two promoters, spyp and ycfSp, were silent in the absence of copper (Fig. 1A).…”

Section: Resultsmentioning

confidence: 99%

“…Of the 13 promoters, 10 promoters, cpxPp, ftnBp, spyp ybaJp1, yccAp, ycfSp, ydeHp, yebEp, yobBp, and yqjAp, were newly determined by this experiment, while three promoters, htrAp, ppiAp, and yihEp, have been reported by others. [22][23][24] The À10 and À35 elements of all 13 promoters were found as typical sequences for recognition by sigma-D (Fig. 3A).…”

Section: Resultsmentioning

confidence: 99%

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Characterization of Copper-Inducible Promoters Regulated by CpxA/CpxR inEscherichia coli

Yamamoto

Ishihama

2006

Bioscience, Biotechnology, and Biochemistry

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The copper stimulon in Escherichia coli consists of four regulons, the CueR-, CusS/CusR-, CpxA/CpxR-, and YedV/YedW regulons. E. coli mutants defective in cpxRA showed higher sensitivity to copper than the wild type. A total of 15 promoters were found to be induced in E. coli culture upon exposure to copper in a CpxA/ CpxR-dependent manner. After gel-shift and DNase I foot-printing analyses, a conserved tandem repeat of pentanucleotide sequence, GTAAA(N) 4{8 GTAAA, with a conserved A of 4-bp upstream of each pentamer, was identified to be the CpxR-binding site. The difference in the orientation and location of the CpxR box is discussed with respect to the regulation mechanism among CpxR-regulon genes.Key words: transcription regulation; CpxA/CpxR; twocomponent system; copper response; Escherichia coliRecently we found that the copper-responsive regulatory system (copper-stimulon) consists of at least four regulons, CueR-, CusSR-, CpxAR-, and YedVW regulons, in E. coli.1) Of a total of 28 copper-inducible genes, 11 were found to belong to the CpxAR regulon.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Characterization of Copper-Inducible Promoters Regulated by CpxA/CpxR inEscherichia coli

Yamamoto

Ishihama

2006

Bioscience, Biotechnology, and Biochemistry

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146

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“…The concentration of Zn(II) used was chosen based on the toxicity experiments, which revealed that 400 μM Zn(II) results in slower growth (as opposed to a lethal concentration leading to no growth). Furthermore, several previous investigations assessing the genome-wide transcriptional response of E. coli to zinc demonstrated that [Zn(II)] >100 μM is sufficient to observe a change in the transcript levels of the above-mentioned transporters, albeit under different media compositions (46,47). While the addition of Zn(II) led to an increase in zntA transcription and a decrease in znuA transcription, as expected, we observed no significant difference between wild type and ΔslyD strains grown in the presence or absence of oxygen (Figures S13 and S15).…”

Section: Impact Of the Slyd Deletion On Transcriptional Metalloregulamentioning

confidence: 99%

Metal Selectivity of the Escherichia coli Nickel Metallochaperone, SlyD

et al. 2011

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SlyD is a Ni(II)-binding protein that contributes to nickel homeostasis in Escherichia coli. The Cterminal domain of SlyD contains a rich variety of metal-binding amino acids, suggesting broader metal-binding capabilities, and previous work demonstrated that the protein can coordinate several types of first row transition metals. However, the binding of SlyD to metals other than Ni(II) has not been previously characterized. To further our understanding of the in vitro metal-binding activity of SlyD and how it correlates with the in vivo function of this protein, the interactions between SlyD and the series of biologically relevant transition metals Mn(II), Fe(II), Co(II), Cu(I) and Zn(II) were examined by using a combination of optical spectroscopy and mass spectrometry. Tables S1-S3 containing a summary of metal concentrations used for metal toxicity studies, a list of primers used for qRT-PCR analysis and summary of Mn(II), Co(II) and Ni(II) stoichiometries of SlyD; Figure S2 shows representative spectra of a Ni(II) titrations analyzed via ESI-MS; Figures S3-S4 shows a graphical representation of the PAR competition assay used for determining the average K D (Zn(II)-SlyD) and a comparison of CD spectra for Ni(II) and Zn(II) bound SlyD. Figure S5 is a representative data set for a Cu(I) titration of SlyD analyzed via electronic absorption spectroscopy. Figure S6-S7 are competition titrations with Bca and Bcs used for determining copper stoichiometry and affinity, respectively. Figure S8-S10 are a graphical representation of Co(II) titrations analyzed via ESI-MS, competition titrations with Fura2 for determining average K D (Co(II)-SlyD) and titration of a cobalt saturated SlyD sample with Zn(II). Figure S11 is spectroscopy data obtained for titration of Ni(II) compared with a similar titration carried out in the presence of excess Fe(II). Figure S12 depicts representative growth curves of WT and ΔslyD strains conducted in minimal media supplemented with various amounts of metal. Figure S13 is relative mRNA levels measured for various metal transporters under aerobic conditions. Figure S14-S15 are relative mRNA levels measured for various metal transporters under anaerobic conditions. This material is available free of charge via the Internet at http://pubs.acs.org.

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“…71) In the presence of excess Zn 2+ , ZntR activates transcription of zntA for export of excess zinc. 63,72) The ZntR-binding site consists of the inverted repeat of ACT-CTGGAGTC.…”

Section: Zntr Transcription Factormentioning

confidence: 99%

“…63,67,72) The Zur-binding site consists of the inverted repeat of GAAATGTTATA with the spacer of mono-nucleotide. 63,67,72) 4.6.3. ZraS-ZraR two-component system.…”

Section: Zur Transcription Factormentioning

confidence: 99%