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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/25 18:51:16」(JST)
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- Deletion of the zupT gene for a zinc importer influences zinc pools in Cupriavidus metallidurans CH34.
- Herzberg M1, Bauer L, Nies DH.Author information 1Molecular Microbiology, University of Halle, Kurt-Mothes-Str. 3, 06099 Halle/Saale, Germany, EU. d.nies@mikrobiologie.uni-halle.de.AbstractCupriavidus metallidurans strain CH34 accomplishes a high level of transition metal resistance by a combination of rather unspecific transition metal import and controlled efflux of surplus metals. Using the plasmid-free mutant strain AE104 that possesses only a limited number of metal efflux systems, cellular metal pools were identified as counterparts of these transport reactions. At low zinc concentrations strain AE104 took up Zn(ii) until the zinc content reached an optimum level of 70 000 Zn(ii) per cell in the exponential phase of growth, whereas a ΔzupT mutant lacking the zinc importer ZupT contained only 20 000 Zn(ii)/cell, possibly the minimum zinc content. Mutant and parent cells accumulated up to 125 000 Zn(ii) per cell at high (100 μM) external zinc concentrations (optimum zinc content). When the mutant strain Δe4, which has all the known genes for zinc efflux systems deleted, was cultivated in the presence of zinc concentrations close to its upper tolerance level (10 μM), these cells contained 250 000 Zn(ii) per cell, probably the maximum zinc content. Instead of zinc, 120 000 cobalt or cadmium ions could also fill-up parts of this zinc pool, showing that it is in fact an undefined pool of divalent transition metal cations bound with low substrate specificity. Even when the cells contained sufficient numbers of total zinc, the zinc importer ZupT was required for important cellular processes, indicating the presence of a pool of tightly bound zinc ions, which depends on ZupT for efficient replenishment. The absence of ZupT led to the formation of inclusion bodies, perturbed oxidative stress resistance and decreased efficiency in the synthesis of the zinc-dependent subunit RpoC of the RNA polymerase, leading to RpoC accumulation. Moreover, when a czc allele for a zinc-exporting transenvelope efflux system CzcCBA was constitutively expressed in a ΔzupT mutant, this led to the disappearance of the CzcA protein and the central subunit of the protein complex, and to the loss of metal resistance. This phenomenon occurred only if the ΔzupT cells had been cultivated for several transfers in solid culture medium, which generated severe zinc starvation. Thus, two zinc pools appear to exist in C. metallidurans: one pool of at least 20 000 tightly bound Zn(ii) ions, in addition to a second pool of up to 200 000 cations bound loosely and with low substrate specificity.
- Metallomics : integrated biometal science.Metallomics.2014 Mar 26;6(3):421-36. doi: 10.1039/c3mt00267e. Epub 2014 Jan 10.
- Cupriavidus metallidurans strain CH34 accomplishes a high level of transition metal resistance by a combination of rather unspecific transition metal import and controlled efflux of surplus metals. Using the plasmid-free mutant strain AE104 that possesses only a limited number of metal efflux system
- PMID 24407051
- Simple Whole-Cell Bio-detection and Bioremediation of Heavy Metals Based on an Engineered Lead-Specific Operon.
- Wei W, Liu X, Sun P, Wang X, Hong Z, Hong M, Mao ZW, Zhao J.AbstractA lead-specific binding protein, PbrR, from the lead resistance operon, pbr, of Cupriavidus metallidurans CH34 was incorporated into E. coli in conjunction with an engineered downstream RFP (red fluorescence protein), which allowed for highly sensitive and selective whole-cell detection of lead ions. The subsequent display of PbrR on the E. coli cell surface permitted selective adsorption of lead ions from media containing various heavy metal ions. The surface-engineered E. coli bacteria effectively protected Arabidopsis thaliana seed germination from the toxicity of lead ions at high concentrations. Engineering the E. coli bacteria harbouring these lead-specific elements from the pbr operon may potentially be a valuable general strategy for bio-detection and bioremediation of toxic heavy metal ions in the environment.
- Environmental science & technology.Environ Sci Technol.2014 Feb 24. [Epub ahead of print]
- A lead-specific binding protein, PbrR, from the lead resistance operon, pbr, of Cupriavidus metallidurans CH34 was incorporated into E. coli in conjunction with an engineered downstream RFP (red fluorescence protein), which allowed for highly sensitive and selective whole-cell detection of lead ions
- PMID 24564581
- Binding of NAD+ and L-Threonine induces Stepwise Structural and Flexibility changes in Cupriavidus Necator L-Threonine Dehydrogenase.
- Nakano S1, Okazaki S, Tokiwa H, Asano Y.Author information 1Toyama Pref. Univ., Japan;AbstractCrystal structures of short chain dehydrogenase-like L-threonine dehydrogenase (SDR-like L-ThrDH) from Cupriavidus necator (CnThrDH) in the apo and holo forms were determined at 2.25 and 2.5 Å, respectively. Structural comparison between the apo and holo forms revealed that four regions of CnThrDH adopted flexible conformations when neither NAD+ nor L-Thr were bound: residues 38-59, residues 77-87, residues 180-186, and the catalytic domain. Molecular dynamics (MD) simulations performed at the 50-nsec timescale revealed that three of these regions remained flexible when NAD+ was bound to CnThrDH: residues 80-87, residues 180-186, and the catalytic domain. MD simulations also indicated that the structure of CnThrDH changed from a closed form to an open form upon NAD+ binding. The newly formed cleft in the open form may function as a conduit for substrate entry and product exit. These computational results led us to hypothesize that the CnThrDH reaction progresses by switching between the closed and open forms. Enzyme kinetics parameters of the L80G, G184A, and T186N variants also supported this prediction: the kcat/Km,L-Thr value of the variants was >330-fold lower than that of the wild type; this decrease suggested that the variants mostly adopt the open form when L-Thr is bound to the active site. These results are summarized in a schematic model of the stepwise changes in flexibility and structure that occur in CnThrDH upon binding of NAD+ and L-Thr. This demonstrates that the dynamical structural changes of SDR-like L-ThrDH are important for the enzyme's reactivity and specificity.
- The Journal of biological chemistry.J Biol Chem.2014 Feb 20. [Epub ahead of print]
- Crystal structures of short chain dehydrogenase-like L-threonine dehydrogenase (SDR-like L-ThrDH) from Cupriavidus necator (CnThrDH) in the apo and holo forms were determined at 2.25 and 2.5 Å, respectively. Structural comparison between the apo and holo forms revealed that four regions of CnThrDH
- PMID 24558034
Japanese Journal
- 2C11-2 Wautersia metallidurans CH34のpoly(3-hydroxybutyrate)結合蛋白質(酵素学・酵素工学・タンパク質工学,一般講演)
- 大庭 全洋,小林 照幸,松崎 智恵子,齊藤 光實
- 日本生物工学会大会講演要旨集 平成17年度, 107, 2005-09-25
- NAID 110007321530
- Biosynthesis of poly-beta-hydroxy-alkanoates by Sphingopyxis chilensis S37 and Wautersia sp. PZK cultured in cellulose pulp mill effluents containing 2,4,6-trichlorophenol
- TOBELLA L.
- J. Ind. Microbiol. Biotechnol. 32, 397-401, 2005
- NAID 30023997870
- Novel intracellular 3-hydroxybutyrate-oligomer hydrolase in Wautersia eutropha H16
- KOBAYASHI T.
- J. Bacteriol. 187, 5129-5135, 2005
- NAID 30021055284
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Related Pictures
★リンクテーブル★
| リンク元 | 「Cupriavidus」「ウォルテルシア属」 |
| 拡張検索 | 「Wautersia eutropha」 |
「Cupriavidus」
カプリアビダス、プリアビダス属、Cupriavidus属