However, Young’s modulus is independent of the applied load when the load is above 10 mN [21]. Moreover, the contact depths in nanostructured samples indented at the lowest peak loads are already equal to or larger than the average grain size, and thus, Young’s modulus does not show any variation with increasing applied load [24]. In order to compare the hardness and modulus of our nanostructured transparent ceramics with those of conventional large-grained ceramics, we averaged the hardness and modulus data shown in Figure 4. The average hardness and modulus are 31.7 and

314 GPa, respectively. Our average hardness is approximately twice that of large-grained (100 to 200 μm) MgAl2O4[25]. This is understandable since the well-known Hall–Petch relationship predicts that a material with a smaller grain size should be harder than the Lenvatinib cell line same material with a larger grain size. Both the average selleck chemicals modulus (314 GPa) and the modulus (265 GPa) measured at the maximum load (9,000 μN) are comparable to the Young’s modulus (277 GPa) of large-grained (100 to 200 μm) MgAl2O4[25]. This is also reasonable since it has been predicted that [26] the difference in Young’s modulus between porosity-free nanostructured materials with a grain size larger than 10 nm and conventional large-grained materials should be within approximately 5%. Conclusion In summary, the deformation behavior and the mechanical

properties (hardness and Young’s modulus) of the nanostructured transparent MgAl2O4 ceramics have been determined by nanoindentation tests. The degree of plastic deformation increases with increasing applied loads. After the indentation test, scanning probe microscope image shows no cracking, whereas high-resolution TEM image shows the evidence of dislocation activity in nanostructured transparent MgAl2O4 ceramics. The measured hardness is much higher than that of conventional large-grained MgAl2O4 ceramics, which should be of considerable interest to the fields of materials science and condensed matter. Acknowledgments This work was check details supported by the National Natural Science Foundation (NSFC) of the People’s Republic of China

under grant no. 50272040, Fok Ying Tong Education Foundation under grant no. 91046, Youth Foundation of Science and Technology of Sichuan Province under grant no. 03ZQ026-03, NSFC of the People’s Republic of China under grant no. 50742046, NSFC of the People’s Republic of China under grant no. 50872083, and Doctor Foundation of Ludong MK-0518 in vivo University under grant no. LY2012019. We thank T.D. Shen for his technical assistance in preparing our manuscript. References 1. Wang C, Zhao Z: Transparent MgAl 2 O 4 ceramic produced by spark plasma sintering. Scripta Mater 2009, 61:193–196.CrossRef 2. Zhang X, Wang Z, Hu P, Han WB, Hong C: Mechanical properties and thermal shock resistance of ZrB 2 –SiC ceramic toughened with graphite flake and SiC whiskers. Scripta Mater 2009, 61:809–812.CrossRef 3.

Figure 7 Simulated diffraction from a slit without corrugations. (a) The near-field and (b) propagated distributions of the magnetic field amplitude |H y | in the neighborhood of a single slit in the Al screen. (c) The field propagating towards and past the image plane z = 0 in an Abbe configuration with numerical aperture 1.4 and magnification × 10. Figure 8 Simulated diffraction from a slit with corrugations. (a) The near-field and (b) propagated https://www.selleckchem.com/products/Trichostatin-A.html distributions of the magnetic field amplitude |H y | in the neighborhood of

a slit surrounded by corrugations. (c) The field propagating towards and past the image plane z = 0 in an Abbe configuration with numerical aperture 1.4 and magnification × 10. The complete field probe with the slit surrounded by corrugations

is considered. Figures 7b and 8b illustrate the fields as they propagate towards the far zone of the slit. In the case of a slit without corrugations, the far zone is effectively reached after a propagation distance of just a few wavelengths, while in the case of the corrugated rear interface, this requires propagation over a few tens of wavelengths. In these illustrations, the entire superperiod is shown in the x direction to illustrate the effectiveness of the PMLs (darker bars on bottom and top) in FMM simulation of non-periodic structures: there is no visible coupling of light from neighboring superperiods near the PML layer, which (if present) would be seen as interference near the darker bars. Finally, Figures 7c and 8c show field distributions in the focal regions of an imaging lens with check details NA = 1.2 and linear magnification of × 10. These results were obtained using Abbe’s

theory of imaging, by retaining only those spatial frequencies of the diffracted field that fall within the NA of the collection lens. The focal fields are symmetric about the geometrical image plane at z = 0. Figure 8c shows clearly the formation of the focus by interference of the incoming narrow light beam and the wide pedestal arriving at larger angles within the image-space numerical aperture. In the case of ID-8 the slit aperture in Figure  7c, the focal spot has only weak side lobes and is essentially diffraction limited. The Peptide 17 manufacturer corrugations increase the side lobe level considerably even at the best focus, indicating that the field immediately behind the exit plane of the probe contains strong phase variations. While the aberrations of grating-based plasmonic collimation systems are worth more careful studies, the increased side lobe level is of little concern in the present application: the area of the detector placed at the image plane can be chosen large enough to capture all side lobes with significant amplitude. In all of the previous simulations, the incident Gaussian beam was assumed to be centered at the slit, but in the experiments, we scanned it in the x direction. We now proceed to simulate the effects of such scanning.

E.M. for the average fold changes. Statistical significance (p < 0.05) between expression following nanomaterial exposure and the controls is denoted by an asterisk (*). Western blot analysis Transgelin 2 protein was analyzed by Western blot in all treatment groups (nano-SiO2, nano-Fe3O4, SWCNTs) Selleckchem Depsipeptide (Figure  4B). Transgelin 2 protein expression was significantly

increased at all doses of nanomaterial exposure compared with the control group (p < 0.05), but there was almost no significant difference between high dose and low dose in nanomaterial exposure groups. Discussion A nanomaterial is a kind of ultrafine material composed of nanosized particles, between 0.01 and 100 nm in diameter. Recently, research and development of these particles have increased [11], and their potential adverse effects are being investigated by researchers around the world [12–14]. Some report that ultrafine particles may cause damage to the body due to their higher activity and selectivity [13]. The effects of ultrafine particles on the lungs have received much more attention. In spite of the lungs being the most direct target organ for such particles, the methods to study lung injury are limited except for histopathobiology, so we attempt to use biochemical analysis and

comparative proteome to detect lung damage in vivo after nanomaterial exposure to find the difference between the nanomaterials see more and non-nanomaterials. We selected the three typical nanomaterials because of their different chemical compositions (nano-SiO2 is an inorganic oxide, nano-Fe3O4 is a metal oxide, and SWCNT is a carbon) and different shapes (nano-SiO2 Oxalosuccinic acid has a crystal structure, nano-Fe3O4 is a sphere, and SWCNT is rope-shaped). In our study, we found that the three nanomaterials induced oxidative damage and

inflammation in BALF. In addition, there are 17 different proteins regardless of the composition and shape of nanomaterials which expressed a similar nanosize. Epidemiologic and experimental animal studies have shown an increased risk of respiratory and cardiovascular morbidity and mortality associated with exposure to ultrafine particles [15, 16]. Nanoparticle exposure induced production of cytokines in lung epithelial cells and in lung tissue [17, 18]. The aim of this study was to characterize the biochemical changes in BALF and protein profiles in the lung tissue of rats following exposure to three nanomaterials using newly available technologies especially comparative proteomics. Higher protein concentrations in the nanomaterial-exposed BALF Niraparib clinical trial samples are likely a result of plasma extravasation. Consistent with this view, many of the plasma-derived proteins identified in both exposed and control samples do indeed change in abundance, for example, albumin [17], but additional work will be required to provide accurate quantification.

By tuning the film thickness and annealing temperature, the density

and the diameters of the holes can be readily controlled. With Ag mesh patterned as catalyst on silicon substrate, fabrication of vertical (100) SiNW arrays with controlled morphologies were achieved, as shown in Figure 4. It is evident that the morphology of SiNWs matches well with the shape of the corresponding holes on the Ag films. It is interesting selleckchem that not only circular (Figure 4b,c) but also quadrate (Figure 4a) cross-sectional SiNWs can be formed using this method. The slight mismatch between the Ag films and the corresponding SiNWs can be attributed to the gradual erosion of the ultrathin Ag film during the etching [18]. selleck chemicals llc Figure 4 SEM images of films with different thicknesses and annealing temperatures and corresponding etching results. (a) The 11-nm-thick Ag film on Si substrate annealed at 120°C for 10 min. (b) The 12-nm-thick Ag film on Si substrate annealed at 160°C for 10 min. (c) The 13-nm-thick Ag film on Si substrate annealed at 175°C for 10 min. Planar and cross-sectional

images of their corresponding etched substrate: (d, g) corresponding to (a), (e, h) corresponding to (b), and (f, i) corresponding to (c). Another important parameter of the SiNW arrays is the length, which can be controlled by varying the etching time. Figure 5b,c,d shows the cross-sectional scanning electron microscope (SEM) images of SiNW arrays fabricated with etching times of 5, 10, and 20 min, respectively. The Ag film is 14 nm and annealed at 150°C for

10 min. As a result, nanowires with lengths of about 0.5 μm, about 1 μm, and about Lonafarnib 2 μm are achieved, respectively. The length of the nanowires shows good linear relationship with the duration of the etching time. The statistical analysis (Figure 5e) shows the good diameter distribution of the as-fabricated SiNWs. Here, the tapered morphology of the nanowires resulted from the gradual Ag dissolution-induced hole size increase. Figure 5 SEM images of plane-view SiNW arrays, cross-sectional SEM images of the SiNWs, and statistical distribution. (a) SEM images of plane-view SiNW arrays achieved with the catalysis of a 14-nm-thick Ag film annealed at 150°C for 10 min and cross-sectional SEM images of the SiNWs etched for (b) 5 min Tyrosine-protein kinase BLK (nanowire length 0.5 μm), (c) 10 min (1 μm), and (d) 20 min (2 μm). All scale bars are 500 nm. (e) The statistical distribution for the average diameters of the corresponding SiNWs. Fabrication of SiNH arrays utilizing Ag nanoparticles When the metal film is annealed at higher temperature, the continuous thin Ag film finally transforms into isolated nanoparticles (Figure 6). As shown in Figure 6a,c, the Ag particles are semispherical and exhibit good distribution and uniformity. The parameters of the nanoparticles can be tuned by varying the film thickness and annealing temperature.

In Kp342 one gene (KPK_A0040) was found on plasmid pKP187 and Selleckchem CAL 101 had a homolog on the chromosome, and two additional genes (KPK_3327 and KPK_2809) had homologs in only one of the other two genomes. PDE activity in K. pneumoniae has been demonstrated only

in a few cases: MrkJ (KP1_4554) and BlrP1 (KPN_01598) [13, 15]. From our analysis it therefore appears that the environmental strain Kp342 has more copies of GGDEF/EAL SBI-0206965 proteins than the clinical isolates. Future studies focused on the function of many of these DGC and PDE genes might shed light on the processes involving growth and survival of this bacterium under different environmental settings. To further analyze the GGDEF proteins in K. pneumoniae, we constructed

a phylogenetic tree using protein sequences from K. pneumoniae and other bacteria (Figure 3). This analysis showed that most of the GGDEF proteins grouped with proteins from other organisms and not with one another. However, KPK_3356, which is unique in the Kp342 genome, was closely related to KPK_A0039 and had 96% amino acid sequence identity. Interestingly, KPK_A0039 is on plasmid pKP187 of the same strain Kp342 [See Additional file 1 and could therefore have resulted from an event of horizontal gene exchange and a transfer between the plasmid and the chromosome. Other unique GGDEF LY411575 proteins in Kp342, like KPK_4891 and KPK_2890, were close to GGDEF proteins from Enterobacter Sitaxentan sp., with more than 96% amino acid sequence identity (Figure 3). The GGDEF proteins KPN_pKPN3p05967 and KPN_pKPN3p05901, found on plasmid pKPN3 of MGH78578, also grouped with GGDEF proteins of Enterobacter sp., whereas pK2044_00660, found on plasmid pK2044 of NTUH-K2044, grouped with GGDEF proteins from Shigella sp. (Figure 3). These results suggest that many of these proteins are phylogenetically related, perhaps because they are derived from a common ancestor or due to horizontal gene

transfer events between K. pneumoniae and other bacteria [37]. Additional studies would need to be carried out to further understand the diversity and distribution of GGDEF proteins in these organisms. Figure 3 Phylogeny of K. pneumoniae GGDEF proteins. The phylogenetic reconstruction was done using neighbor-joining with 73 amino acid sequences from K. pneumoniae GGDEF proteins and other bacteria. Nodes with less than 70% support after 1000 bootstrap replicates are indicated with an asterisk. GGDEF proteins from Kp342, MGH78578 and NTUH-K2044 are highlighted in purple. Arrowheads represent the unique GGDEF proteins found in the K. pneumoniae strains 3 genomic and 3 plasmic encoded copies. The scale bar indicates the number of amino acid substitutions per site. Conclusions As in other enteric bacteria, K. pneumoniae harbored multiple copies of GGDEF and EAL-containing proteins.

420 m, branch of Quercus petraea 2 cm thick, 24 Sep. 2005, H. Voglmayr, W.J. 2859 (WU 24059). Melk, Leiben, Weitental, at Hofmühle, MTB 7757/2, 48°14′51″ N, 15°17′23″ E, elev. 270 m, partly decorticated branch of Fagus sylvatica 6 cm thick, soc. Tubeufia cerea (on ?Diatrype decorticata), Lasiosphaeria

hirsuta, Hypoxylon cohaerens, Lopadostoma turgidum, Orbilia inflatula, Corticiaceae, 25 Jul. 2004, H. Voglmayr & W. Jaklitsch, W.J. 2539 (WU 24049, culture C.P.K. 1910). Melk, Sankt Leonhard am Forst, 2 km before Großweichselbach towards Melk, MTB 7857/2, 48°09′42″ N, 15°17′36″ E, elev. 285 m, on partly decorticated branch of Quercus petraea 3–4 cm thick, soc. effete Diatrypella quercina, Phellinus ferruginosus, 30 Sep. 2004, W. Jaklitsch, W.J. 2748 (WU 24056, culture CBS 118979 = C.P.K.

1917). Wienerwald, Kaltenleutgeben, near Stangau, MTB 7862/4, Ro 61-8048 order 48°06′20″ N, 16°08′12″ E, elev. 450 m, on thick branch of Quercus cerris, 5 Oct. 2008, W. Jaklitsch & O. Sükösd, 5 Oct. 2008, W.J. 3220 (WU 29224). Wien-Umgebung, Mauerbach, walking path from the cemetery, MTB 7763/1, 48°15′19″ N, 16°10′13″ E, elev. 330 m, on a log segment of Carpinus betulus on moist ground in leaf litter, soc. Steccherinum ochraceum, 23 Jul. 2005, W. Jaklitsch, W.J. 2820 (WU 24057, culture PSI-7977 molecular weight C.P.K. 2134). Same area, 48°15′18″ N, 16°10′10″ E, elev. 325 m, on decorticated branch of Fagus sylvatica 8 cm thick, on wood, soc. Bertia moriformis, Hypoxylon fragiforme, 7 Oct. 2006, W. Jaklitsch & H. Voglmayr, W.J. 3002 (WU 29217). Pressbaum, Rekawinkel, forest path south of the train station, MTB 7862/1, 48°10′47″ N, 16°02′03″ E, Rolziracetam elev. 360 m, on corticated branch of Alnus glutinosa 5 cm thick, holomorph, soc. a myxomycete, effete ?Diatrypella, 18 Oct. 2003, H. Voglmayr & W. Jaklitsch, W.J. 2476 (WU 24047, culture C.P.K. 2133). Oberösterreich, Schärding, St.

Willibald, Großer Salletwald, MTB 7648/3, 48°20′57″ N, 13°42′22″ E, elev. 660 m, on corticated branch of Fagus sylvatica on the ground, soc. old Corticiaceae, 26 Oct. 2005, H. Voglmayr, W.J. 2866 (WU 24061). Großer Salletwald, MTB 7648/1, elev. 455 m, on branch of Fagus sylvatica, 13 Aug. 2006, H. Voglmayr, W.J. 2928 (WU 29215, culture C.P.K. 3117). Steiermark, Graz-Umgebung, Mariatrost, BLZ945 Wenisbucher Straße, MTB 8858/4, 47°06′40″ N, 15°29′11″ E, elev. 470 m, on a 4–5 cm thick branch of a large dead tree of Fagus sylvatica, lying on the ground, 20 Aug. 2004, W. Jaklitsch, W.J. 2611 (WU 24054, culture C.P.K. 1915). Tirol, Innsbruck-Land, Ampass, Ampasser Hügel, MTB 8734/2, 47°15′31″ N, 11°27′16″ E, elev. 720 m, on decorticated branch of Alnus incana 2 cm thick, on ground among moss; holomorph, soc. Nemania serpens, Stereum subtomentosum, 2 Sep. 2003, U. Peintner & W. Jaklitsch, W.J. 2354 (WU 24043, culture C.P.K. 944). Vorarlberg, Feldkirch, Rankweil, behind the hospital Valduna, MTB 8723/2, 47°15′40″ N, 09°39′00″ E, elev.

Haem-staining analysis E. meliloti cells grown aerobically in 150 ml of TY medium were harvested selleck by centrifugation at 8000 g for 5 min, washed twice with MM, resuspended in 200 ml of MM or

MMN at an OD600 of 0.15-0.2 and incubated under 2% initial O2 or anoxic (filled bottles) conditions for 24 h. The cell pellets were resuspended in 3 ml of 50 mM potassium phosphate buffer (pH 7) containing 100 μM 4-(2-aminoethyl) benzene-sulfonyl fluoride hydrochloride (ABSF), RNAse (20 μg · ml-1) and DNAse I (20 μg · ml-1). The cells were disrupted using a French pressure cell at a constant pressure of approximately 1000 psi (SLM Aminco, Jessup, MD, USA). The cell extract was centrifuged at 10,000 g for 20 min to remove the unbroken cells, and the supernatant was centrifuged at 140,000 g for 1 h. The membrane pellet was resuspended in 100 μl of the same buffer. The membrane

protein aliquots were diluted in sample buffer [124 mM Tris–HCl, pH 7.0, 20% glycerol, 4.6% sodium dodecyl sulphate (SDS) and 50 mM 2-mercaptoethanol] and incubated at room temperature for 10 min. The membrane proteins were separated at 4°C using 12% SDS-polyacrylamide gel electrophoresis, 4SC-202 chemical structure transferred to a nitrocellulose membrane and stained for haem-dependent peroxidase activity, as described previously [45], using the SuperSignal chemiluminescence detection kit (Pierce, Thermo Fisher Scientific, IL, USA). Analytical methods The nitrite JQ-EZ-05 mouse concentration was estimated after diazotisation by adding the sulphanilamide/naphthylethylene diamine dihydrochloride reagent [46]. The protein concentration was estimated using the Bradford method (Bio-Rad Laboratories, Richmond, CA) with a standard curve constructed with varying bovine serum albumin concentrations. Nitric oxide determination E. meliloti cells were incubated at an OD600 of 0.15-0.2 in MMN under 2% initial O2 or anoxic conditions, harvested and washed similar to the NR or Nir activity assays. Nitric oxide was measured amperometrically with a 2-mm ISONOP electrode APOLO 4000® (World Precision Inst., Sarasota, FL, USA) in

a 3-ml thermostatted and magnetically stirred reaction chamber [47]. The membrane-covered electrode was situated at the Acyl CoA dehydrogenase bottom of the chamber above the stirrer, and the reactants were injected using a Hamilton syringe through a port in the glass stopper. To determine the net production of NO, the 3-ml cuvette was filled with 1.410 ml of 25 mM phosphate buffer (pH 7.4), 250 μl (0.1-0.2 mg protein) of a cellular solution, 100 μl of an enzymatic mix containing glucose oxidase (Aspergillus niger) (80 units/2 ml) and catalase (bovine liver) (500 units/2 ml), 90 μl of 1 M sodium succinate and 100 μl of 320 mM glucose. When oxygen was consumed and a steady base line was observed, 50 μl of 1 M NaNO2 was added to the cuvette to begin the reaction. Each assay was continued until NO was detected.

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Co-infection experimental design Vero cells, an African green monkey kidney cell line (ATCC CRL 1587), were used for all infection experiments. They were propagated in GM without gentamycin Foretinib nmr at 37°C in an atmosphere of 5% CO2. Vero cells were divided into four groups: for mock infection, chlamydial infection, ca-PEDV infection, and both Chlamydia and ca-PEDV double infection. Host cells were infected with a MOI of 1 for Chlamydia and an infective dose of 1 × 105,5 TCID50/ml for ca-PEDV, respectively. For ca-PEDV monoinfections and negative controls, infection medium was used. All co-infection experiments were done three times and monoinfections with Chlamydia and ca-PEDV

were performed simultaneously. The optimal experimental protocol (adding the virus several hours after chlamydial infection) for co-infection procedure was developed before (data not shown). For dual infections, cell monolayers were first

infected with Chlamydia at a MOI of 1. All coverslips were centrifuged at 1000 × g for 1 h at 25°C. Timepoint 0 (T0) was defined after centrifugation and supernatant was replaced subsequently LY2874455 by incubation medium. Infected monolayers were then incubated for 14 h at 37°C (T0 – T14). All cell layers for dual infections or ca-PEDV monoinfection were exposed to a ca-PEDV suspension (1 × 105,5 TCID50), the samples were centrifuged again for 1000 × g for 1 h at 25°C and incubated for 24 h at 37°C. After this incubation period, all monolayers were fixed and further investigated by FK506 in vitro Indirect immunofluorescence and transmission electron microscopy. Re-infection experiments were performed to compare the production of infectious chlamydial elementary bodies (EBs) between monoinfections and mixed infections. Indirect Immunofluorescence For indirect immunofluorescence analyses, infected cells were fixed in absolute methanol (-20°C) for 10 min. and IF labeling

of cell cultures was performed immediately Morin Hydrate after fixation. For viral antigen detection, a mouse monoclonal antibody against the M protein of PEDV (mcAb 204, kindly provided by Prof. Dr. M. Ackermann, Institute of Virology, University of Zurich), diluted 1:4 in PBS supplemented with BSA, and an Alexa Fluor 594-conjugated secondary antibody (goat anti-mouse, 1:500, Molecular Probes, Eugene, USA) were used. Chlamydial inclusions were labeled with a Chlamydiaceae family-specific mouse monoclonal antibody directed against the chlamydial lipopolysaccharide (mLPS; Clone ACI-P, Progen, Heidelberg, Germany) and a secondary Alexa Fluor 488-conjugated secondary antibody (goat anti-mouse, 1:500, Molecular Probes). DNA was labeled with 1 μg/ml 4′, 6-Diamidin-2′-phenylindoldihydrochlorid (DAPI, Molecular Probes). All staining procedures were conducted at room temperature.

The [γ-32P]-labeled upstream region of each genes (10 fmol of target DNA probes) were incubated with the purified Zur protein in the presence of 100 μM ZnCl2. 0, 1.25, 2.5, 5, 5, 5 and 0 pmol of Zur were used in lanes 1 to 4 and C1 to C3, respectively. The mixtures were directly subjected to 4% polyacrylamide gel electrophoresis. For lanes 1 to 4, the retarded DNA band with decreased mobility turned up, which presumably represented the Zur-DNA complex. To confirm the specificity of the HSP inhibitor binding complexes, either a 200-fold molar excess of DNA Damage inhibitor nonspecific competitor (2 pmol of unlabeled znuA DNA without its predicted binding region in lane C1) or a 200-fold molar excess of specific competitor (2 pmol

of unlabeled target DNA probe in lane C2) was added to the binding mixture. 2 pmol of an unrelated protein, i.e., purified rabbit anti-F1 antibody, were included in lane C3. Both znuA and znuC gave positive EMSA results. Since these two genes had overlapped upstream regions and shared a single predicted Zur site, the EMSA data of only znuA rather than znuC was presented herein. The EMSA experiments still included three additional VX-661 in vivo genes, astC, astA and rovA (Fig. 3). As expected, the negative control rovA gave negative EMSA result. astC and astA were the first and second genes of the astCADBE operon, respectively. The whole operon was induced by Zur

as determined by cDNA microarray, and real-time RT-PCR confirmed the up-regulation of astC by Zur (Additional file 5). astA gave a high score value (8.2) in the computational promoter analysis, while astC presented a

very low value of 4.4 (Table 1). Both of astC and astA gave the negative EMSA results (Fig. 3). Herein, neither astCADB nor astADB was thought to be under the direct control of Zur by directly binding to a cis-acting element within corresponding upstream promoter region. Zur represses promoter activity of znuA, znuCB and ykgM-rpmJ2 To further validate the effect of Zur on the promoter activity of znuCB, znuA and ykgM-rpmJ2, we constructed oxyclozanide the znuC::lacZ, znuA::lacZ and ykgM::lacZ fusion promoters each consisting of an upstream DNA of the corresponding gene, and then each of them was transformed into WT and Δzur, respectively. The β-galactosidase production of these lacZ fusions was measured in both WT and Δzur, which represented the promoter activity of the corresponding gene in each strain. It should be noted that the zur mutation had an effect on the copy number of recombinant or empty pRS551 plasmid, and accordingly a normalized Miller unit was used to calculate the fold change in the activity of each fusion promoter in Δzur in relative to WT (Table 2). For each of the three genes, there was a significant increase of β-galactosidase activity in Δzur compared to WT when they grew in TMH with the addition of zinc. Thus, Zur repressed the promoter activities of znuC, znuA and ykgM.