Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity response of the antioxidant enzymes superoxide dismutase, catalase, ATP enzyme activities of Escherichia coli (G-), Bacillus subtilis (G+), and Burkholderia cepacia WZ1 (G-) following exposure to quinclorac was investigated. The bacterial strains were treated with the different concentrations of quinclorac (1.65, 16.5, 33.0, 165.0, 330.0, and 500.0 microg L(-1)). Results obtained indicated that SOD and CAT activities of these bacteria were induced positively and obviously by quinclorac, especially to gram-positive (G+) bacteria treated by lower than 330 microg L(-1) of quinclorac. The inhibition of ATPase in E. coli K12, B. subtilis, and B. cepacia WZ1 appeared stronger with the increase of quinclorac concentration, showing a striking dose response relationship, which can, therefore, be used as an available bioindicator for quinclorac pollution. The concentration of quinclorac applied in this research had significant effects on these three bacteria at the early stage of incubation, but none of which was persistent. Native polyacrylamide gel electrophoresis and activity staining of SOD revealed that quinclorac had effects on isoforms of E. coli and B. subtilis, and on the staining intensities of the isoforms of B. cepacia WZ1. When E. coli K12 was incubated with 330 microg L(-1) of quinclorac, the upper band of the isoforms of SOD tended to become slightly more apparent at 1 h after the quinclorac treatment, but the staining activity was slightly reduced after the prolonged treatment of quinclorac. No such changes of the isoforms of B. cepacia WZ1 was observed.
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PMID:The response of Escherichia coli, Bacillus subtilis, and Burkholderia cepacia WZ1 to oxidative stress of exposure to quinclorac. 1518 32

The coherent electromagnetic radiation (EMR) of the frequency of 51.8 and 53 GHz with low intensity (the power flux density of 0.06 mW/cm(2)) affected the growth of Escherichia coli K12(lambda) under fermentation conditions: the lowering of the growth specific rate was considerably (approximately 2-fold) increased with exposure duration of 30-60 min; a significant decrease in the number of viable cells was also shown. Moreover, the enforced effects of the N,N'-dicyclohexylcarbodiimide (DCCD), inhibitor of H(+)-transporting F(0)F(1)-ATPase, on energy-dependent H(+) efflux by whole cells and of antibiotics like tetracycline and chloramphenicol on the following bacterial growth and survival were also determined after radiation. In addition, the lowering in DCCD-inhibited ATPase activity of membrane vesicles from exposed cells was defined. The results confirmed the input of membranous changes in bacterial action of low intensity extremely high frequency EMR, when the F(0)F(1)-ATPase is probably playing a key role. The radiation of bacteria might lead to changed metabolic pathways and to antibiotic resistance. It may also give bacteria with a specific role in biosphere.
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PMID:Extremely high frequency electromagnetic radiation enforces bacterial effects of inhibitors and antibiotics. 1863 80

Examining global effects of toxins on gene expression profiles is proving to be a powerful method for toxicity assessment and for investigating mechanisms of toxicity. This study demonstrated the application of prokaryotic real-time gene expression profiling in Escherichia coli for toxicity assessment of environmental pollutants in water samples, by use of a cell-array library of 93 E. coli K12 strains with transcriptional green fluorescent protein (GFP) fusions covering most known stress response genes. The high-temporal-resolution gene expression data, for the first time, revealed complex and time-dependent transcriptional activities of various stress-associated genes in response to mercury and mitomycin (MMC) exposure and allowed for gene clustering analysis based on temporal response patterns. Compound-specific and distinctive gene expression profiles were obtained for MMC and mercury at different concentrations. MMC (genotoxin) induced not only the SOS response, which regulates DNA damage and repair, but also many other stress genes associated with drug resistance/sensitivity and chemical detoxification. A number of genes belonging to the P-type ATPase family and the MerR family were identified to be related to mercury resistance, among which zntA was found to be up-regulated at an increasing level as the mercury concentration increased. A mechanism-based evaluation of toxins based on real-time gene expression profiles promises, to be an efficient and informative method for toxicity assessment in environmental samples.
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PMID:Prokaryotic real-time gene expression profiling for toxicity assessment. 1960 79

To understand the importance of selected regions of the regulatory light chain (RLC) for phosphorylation-dependent regulation of smooth muscle myosin (SMM), we expressed three heavy meromyosins (HMMs) containing the following RLC mutants; K12E in a critical region of the phosphorylation domain, GTDP(95-98)/AAAA in the central hinge, and R160C a putative binding residue for phosphorylated S19. Single-turnover actin-activated Mg(2+)-ATPase (V(max) and K(ATPase)) and in vitro actin-sliding velocities were examined for both unphosphorylated (up-) and phosphorylated (p-) states. Turnover rates for the up-state (0.007-0.030 s(-1)) and velocities (no motion) for all constructs were not significantly different from the up-wild type (WT) indicating that they were completely turned off. The apparent binding constants for actin in the presence of ATP (K(ATPase)) were too weak to measure as expected for fully regulated constructs. For p-HMM containing GTDP/AAAA, we found that both ATPase and motility were normal. The data suggest that the native sequence in the central hinge between the two lobes of the RLC is not required for turning the HMM off and on both kinetically and mechanically. For p-HMM containing R160C, all parameters were normal, suggesting that R160C is not involved in coordination of the phosphorylated S19. For p-HMM containing K12E, the V(max) was 64% and the actin-sliding velocity was approximately 50% of WT, suggesting that K12 is an important residue for the ability to sense or to promote the conformational changes required for kinetic and mechanical activation.
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PMID:Kinetic and motor functions mediated by distinct regions of the regulatory light chain of smooth muscle myosin. 1963 97

Dynamic oscillation of the Min system in Escherichia coli determines the placement of the division plane at the midcell. In addition to stimulating MinD ATPase activity, we report here that MinE can directly interact with the membrane and this interaction contributes to the proper MinDE localization and dynamics. The N-terminal domain of MinE is involved in direct contact between MinE and the membranes that may subsequently be stabilized by the C-terminal domain of MinE. In an in vitro system, MinE caused liposome deformation into membrane tubules, a property similar to that previously reported for MinD. We isolated a mutant MinE containing residue substitutions in R10, K11 and K12 that was fully capable of stimulating MinD ATPase activity, but was deficient in membrane binding. Importantly, this mutant was unable to support normal MinDE localization and oscillation, suggesting that direct MinE interaction with the membrane is critical for the dynamic behavior of the Min system.
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PMID:Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli. 2002 70

It has been shown that the exposure of wild-type Escherichia coli K12 bacteria grown in anaerobic conditions upon fermentation of glucose to coherent extremely high-frequency (51.8 and 53 GHz) electromagnetic radiation (EMR) or millimeter waves (wavelength 5.8 to 6.7 mm) of low intensity (flux capacity 0.06 mW/cm2) caused a marked decrease in energy-dependent and N,N'-dicyclohexylcarbodiimide- or azide-sensitive proton and potassium ions transport fluxes through the membrane, including proton fluxes via proton F0F1-ATPase and through the potassium uptake Trk system, correspondingly. K+ uptake was less for the E. coli mutant Trk 1110. The rate of molecular hydrogen production by formate hydrogen lyase 2 is strongly inhibited. The results indicate that the bacterial effect of coherent extremely high-frequency EMR includes changes in the activity of membrane transport and enzymatic systems in which the F0F1-ATPase plays a key role.
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PMID:[Effect of coherent extremely high-frequency and low-intensity electromagnetic radiation on the activity of membrane systems in Escherichia coli]. 2006 87

The Escherichia coli RecQ DNA helicase participates in a pathway of DNA repair that operates in parallel to the recombination pathway driven by the multisubunit helicase-nuclease machine RecBCD. The model mycobacterium Mycobacterium smegmatis executes homologous recombination in the absence of its helicase-nuclease machine AdnAB, though it lacks a homolog of E. coli RecQ. Here, we identify and characterize M. smegmatis RqlH, a RecQ-like helicase with a distinctive domain structure. The 691-amino acid RqlH polypeptide consists of a RecQ-like ATPase domain (amino acids 1-346) and tetracysteine zinc-binding domain (amino acids 435-499), separated by an RqlH-specific linker. RqlH lacks the C-terminal HRDC domain found in E. coli RecQ. Rather, the RqlH C-domain resembles bacterial ComF proteins and includes a phosphoribosyltransferase-like module. We show that RqlH is a DNA-dependent ATPase/dATPase that translocates 3'-5' on single-stranded DNA and has 3'-5' helicase activity. These functions inhere to RqlH-(1-505), a monomeric motor unit comprising the ATPase, linker and zinc-binding domains. RqlH homologs are distributed widely among bacterial taxa. The mycobacteria that encode RqlH lack a classical RecQ, though many other Actinobacteria have both RqlH and RecQ. Whereas E. coli K12 encodes RecQ but lacks a homolog of RqlH, other strains of E. coli have both RqlH and RecQ.
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PMID:Mycobacterium smegmatis RqlH defines a novel clade of bacterial RecQ-like DNA helicases with ATP-dependent 3'-5' translocase and duplex unwinding activities. 2228 22

The effects of low intensity (flux capacity 0.06 mW/cm2) coherent electromagnetic irradiation (EMI) of 70.6 and 73 GHz frequencies and their combined effects with antibiotics--ceftriaxone or kanamycin (0.4 or 15 microM, correspondingly) on E. coli K12 growth and survival have been reported previously. To further study the effects of EMI and antibiotics and mechanisms, decrease in overall energy (glucose)-dependent H+ and K+ fluxes across the cell membrane was investigated in E. coli. The depression of H+ and K+ fluxes rate was maximally achieved with the 73 GHz frequency. The EMI strengthened the effect of N,N'-dicyclohexycarbodiimide (DCCD, an inhibitor of the F0F1-ATPase). The 73 GHz EMI had more influence on H+ efflux inhibition, whereas 70.6 GHz on K+ influx. Also, EMI strengthened the depressive effects of ceftriaxone and kanamycin on the overall and DCCD-inhibited H+ and K+ fluxes. The 73 GHz EMI strengthened the effect of ceftriaxone on both ions fluxes. Kanamycin depressed H+ efflux more as compared to ceftriaxone, which was also strengthened with EMI. The results of E. coli H+ and K+ transport systems activities depression by irradiation and the irradiation effect on DCCD and antibiotics action indicated the EMI and antibiotics causing primary changes in the bacterial membrane.
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PMID:Effects of low intensity electromagnetic irradiation of 70.6 and 73 GHz frequencies and antibiotics on energy-dependent proton and potassium ion transport by E. coli. 2335 Feb 77

ATAD2 (ATPase family AAA domain-containing protein 2) is a chromatin regulator harboring an AAA+ ATPase domain and a bromodomain, previously proposed to function as an oncogenic transcription co-factor. Here we suggest that ATAD2 is also required for DNA replication. ATAD2 is co-expressed with genes involved in DNA replication in various cancer types and predominantly expressed in S phase cells where it localized on nascent chromatin (replication sites). Our extensive biochemical and cellular analyses revealed that ATAD2 is recruited to replication sites through a direct interaction with di-acetylated histone H4 at K5 and K12, indicative of newly synthesized histones during replication-coupled chromatin reassembly. Similar to ATAD2-depletion, ectopic expression of ATAD2 mutants that are deficient in binding to these di-acetylation marks resulted in reduced DNA replication and impaired loading of PCNA onto chromatin, suggesting relevance of ATAD2 in DNA replication. Taken together, our data show a novel function of ATAD2 in cancer and for the first time identify a reader of newly synthesized histone di-acetylation-marks during replication.
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PMID:ATAD2 is an epigenetic reader of newly synthesized histone marks during DNA replication. 2761 20

Proteolysis is a vital mechanism to regulate the cellular proteome in all kingdoms of life, and ATP-dependent proteases play a crucial role within this process. In Escherichia coli, ClpYQ is one of the primary ATP-dependent proteases. In addition to function with removals of abnormal peptides in the cells, ClpYQ degrades regulatory proteins if necessary and thus let cells adjust to various environmental conditions. In E. coli, SulA, RcsA, RpoH and TraJ as well as RNase R, have been identified as natural protein substrates of ClpYQ. ClpYQ contains ClpY and ClpQ. The ATPase ClpY is responsible for protein recognition, unfolding, and translocation into the catalytic core of ClpQ. In this study, we use an indirect identification strategy to screen possible ClpY targets with E. coli K12 proteome chips. The chip assay results showed that YbaB strongly bound to ClpY. We used yeast two-hybrid assay to confirm the interactions between ClpY and YbaB protein and determined the K_d between ClpY and YbaB by quartz crystal microbalance. Furthermore, we validated that YbaB was successfully degraded by ClpYQ protease activity using ClpYQ in vitro and in vivo degradation assay. These findings demonstrated the YbaB is a novel substrate of ClpYQ protease. This work also successfully demonstrated that with the use of recognition element of a protease can successfully screen its substrates by indirect proteome chip screening assay.
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PMID:Escherichia coli Proteome Microarrays Identified the Substrates of ClpYQ Protease. 2786 22


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