Graduate School of Biomedical Sciences
Joseph Capecci
University of Medicine and Dentistry of New Jersey
Lon Protease is Involved in the Paradoxical Effect of Escherichia Coli Exposed to High Quinolone Con
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Lon Protease is Involved in the Paradoxical Effect of Escherichia Coli Exposed to High Quinolone Concentration
Author : Joseph Capecci
Publisher : University of Medicine and Dentistry of New Jersey, Graduate School of Biomedical Sciences
Published : 2008
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ISBN-13 :
Number of Pages : 140 Pages
Language : en
Descriptions Lon Protease is Involved in the Paradoxical Effect of Escherichia Coli Exposed to High Quinolone Concentration
Read Online Lon Protease is Involved in the Paradoxical Effect of Escherichia Coli Exposed to High Quinolone Concentration pdf
Download Lon Protease is Involved in the Paradoxical Effect of Escherichia Coli Exposed to High Quinolone Concentration epub
Lon Protease is Involved in the Paradoxical Effect of Escherichia Coli Exposed to High Quinolone Concentration Audiobook Download
Listen Lon Protease is Involved in the Paradoxical Effect of Escherichia Coli Exposed to High Quinolone Concentration book
Download Lon Protease is Involved in the Paradoxical Effect of Escherichia Coli Exposed to High Quinolone Concentration Audiobook
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Results Lon Protease is Involved in the Paradoxical Effect of Escherichia Coli Exposed to High Quinolone Concentration
Lon protease inactivation, or translocation of the - Introduction. The misuse and overuse of antibiotics has led to an alarming emergence and spread of resistant pathogens. In Europe and the USA alone, drug-resistant pathogens lead to an estimated excess of 25 000 and 23 000 deaths and 1.5 billion euros and 20 billion dollars in health care expenses each year respectively (ECDC/EMEA Joint technical report, The bacterial challenge: time to react
Molecular insights into substrate recognition and ... - eLife - The Lon AAA+ protease (LonA), previously known as the protease La, is an ATP-dependent protease distributed in prokaryotes and eukaryotes (Charette et al., 1981).It forms a homo-hexamer to execute its biological function (Park et al., 2006; Goldberg et al., 1994).LonA belongs to the AAA+ (ATPases associated with various cellular activities) superfamily and contains an N-terminal domain (NTD
Mitochondrial Lon protease is a gatekeeper for proteins newly ... - Nature - a Domain architecture of the Lon protease: an N-terminal domain, a central AAA + ATPase domain and a C-terminal protease domain. The AAA + domain consists of two subdomains, Walker A and Walker B
Lon protease is essential for paradoxical survival of Escherichia coli - A deficiency of the Escherichia coli Lon protease blocked paradoxical survival occurring at very high nalidixic acid concentrations. The absence of Lon also blocked a parallel increase in cell lysate viscosity likely to reflect DNA size. Thus, Lon may participate in repairing quinolone-mediated DNA lesions formed at high drug concentrations
Lon protease promotes survival of Escherichia coli during anaerobic - To directly assess the effect of Lon protease deficiency on stationary-phase survival, we switched from BL21(DE3) to wild-type K-12. (E. coli B strains are naturally Lon protease-deficient; Donch and Greenberg 1968.) To avoid effects of metabolic products and variation in the media on surviving starvation, cells were harvested from 24 h aerobic
Effects of Lon protease down-regulation on the mitochondrial function - The Lon protease is an ATP-dependent protease of the mitochondrial matrix that contributes to the degradation of abnormal and oxidized proteins in this compartment. It is also involved in the stability and regulation of the mitochondrial genome. The effects of a depletion of this protease on the mitochondrial function and the identification of
Lon protease: a novel mitochondrial matrix protein in the - Lon, a matrix protease involved in protein and mtDNA quality control, was up-regulated at mRNA and protein levels under all conditions. However, only efavirenz decreased the mitochondrial content of Lon while increasing its extramitochondrial presence and its localization to MAMs. ... This latter effect resulted in an enhanced mitochondria/ER
An Integrated Proteomic Approach Uncovers Novel Substrates and ... - PubMed - In Escherichia coli, the ATP-dependent Lon protease is crucial for protein quality control and regulatory processes. To understand how diverse substrates are selected and degraded, unbiased global approaches are needed. We employed a quantitative Super-SILAC (stable isotope labeling with amino acids in cell culture) mass spectrometry approach
Effect of Lon protease knockdown on mitochondrial function in HeLa - Among these proteolytic systems, Lon protease is involved in the control of selective protein turnover in the mitochondrial matrix. ... [18], [19], [20]. Few studies investigated the effects of Lon down-regulation in human cells [9], [16], [21], [22], [23]. We have recently shown that Lon activity declines in old yeast and that Lon deficiency
Mitochondrial Lon protease at the crossroads of oxidative stress - Lon protease is a nuclear DNA-encoded mitochondrial enzyme highly conserved throughout evolution, involved in the degradation of damaged and oxidized proteins of the mitochondrial matrix, in the correct folding of proteins imported in mitochondria, and in the maintenance of mitochondrial DNA. Lon expression is induced by various stimuli, including hypoxia and reactive oxygen species, and
Lon protease inactivation in Drosophila causes unfolded ... - Nature - Creation of Lon-deficient Drosophila strains. To explore the biological roles of Lon protease we used CRISPR/Cas9 technology to create a null allele of the Drosophila Lon gene (CG8798).Briefly, we
Lon protease family - Wikipedia - In molecular biology, the Lon protease family is a family of enzymes that break peptide bonds in proteins resulting in smaller peptides or amino acids. [1] They are found in archaea, bacteria and eukaryotes. Lon proteases are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (Lon protease family, clan SJ)
A Conserved Domain in Escherichia coli Lon Protease Is Involved in - Lon protease of Escherichia coli regulates a diverse set of physiological responses including cell division, capsule production, plasmid stability, and phage replication. Little is known about the mechanism of substrate recognition by Lon. To examine the interaction of Lon with two of its substrates, RcsA and SulA, we generated point mutations in lon which affected its substrate specificity
Lon Protease Is Essential for Paradoxical Survival of Escherichia coli - The effect is blocked by a deficiency of the Lon protease (Malik, Capecci and Drlica 2009) and is not observed in the recA mutant, where the degree of CFU reduction by the antibiotic is
Inactivation of Lon protease reveals a link between ... - Nature - Overexpression of another matrix-localized AAA + protease, ClpP, partially rescued a behavioral deficit of Lon knockdown flies, suggesting that ameliorating the accumulation of unfolded proteins
Lon Protease Is Essential for Paradoxical Survival of - Paradoxical survival in the presence of chloramphenicol. An exponentially growing culture of strain KD2140 (gyrA67 gyrB225) was treated with 20 μg/ml chloramphenicol for 10 min prior to addition of the indicated concentrations of nalidixic acid for an additional 180 min, at which time samples were diluted, applied to drug-free agar, and incubated to determine bacterial survival
Lon Protease Is Essential for Paradoxical Survival of Escherichia coli - A deficiency of the Escherichia coli Lon protease blocked paradoxical survival occurring at very high nalidixic acid concentrations, suggesting Lon may participate in repairing quinolone-mediated DNA lesions formed at high drug concentrations. ABSTRACT A deficiency of the Escherichia coli Lon protease blocked paradoxical survival occurring at very high nalidixic acid concentrations
Lon protease negatively affects GacA protein stability and expression - However, little is known about its underlying molecular mechanisms. In this study, we demonstrated that Lon protease, a member of the ATP-dependent protease family, negatively regulated the Gac/Rsm cascade. In a lon mutant, the steady-state levels and the stability of the GacA protein were significantly elevated at the end of exponential growth
Effects of Lon protease down-regulation on the mitochondrial ... - PubMed - The Lon protease is an ATP-dependent protease of the mitochondrial matrix that contributes to the degradation of abnormal and oxidized proteins in this compartment. It is also involved in the stability and regulation of the mitochondrial genome. The effects of a depletion of this protease on the mit …
PDF Inhibition of Lon protease by bacterial lipopolisaccharide (LPS) though - Lon protease, an ATP-dependent protease in . Esche - richia coli, degrades abnormal proteins and regulates ... Lon protease of . E. coli. is involved in the acquisition of tolerance to UV or high pressure, bacteriophage devel- ... effects on the activities of Lon. 2. MATERIALS AND METHODS . 2.1. Materials . Lipopolysaccharide (LPS; E. coli
PDF Lon Protease Is Essential for Paradoxical Survival of Escherichia coli - vival similar to the wild-type strain (Fig. 2B). Thus, paradoxical survival requires Lon activity but not through its effect on SulA stability. Lon protease has multiple domains, one functioning as an
Lon protease is essential for paradoxical survival of Escherichia coli - A deficiency of the Escherichia coli Lon protease blocked paradoxical survival occurring at very high nalidixic acid concentrations. The absence of Lon also blocked a parallel increase in cell lysate viscosity likely to reflect DNA size. ... In the present case, we observed the Lon effect only at very high concentrations of nalidixic acid
Complete three-dimensional structures of the Lon protease translocating - Lon is a large multidomain protein that assembles into a homohexamer ().The N-terminal region contains a bilobal globular domain (7-10), which recognizes and binds protein substrates (11-13), followed by a 40-residue C-terminal linker with unknown structural and functional fused AAA+ and the protease domains form a hexameric core complex (14-18), which carries out ATP-dependent
Lon protease: a novel mitochondrial matrix protein in the - Markers of mitochondrial dynamics (dynamin-related protein 1, optic atrophy 1 and mitofusin 2) were expressed differently with these stimuli, pointing to a specificity of combined ER/mitochondrial stress. Lon, a matrix protease involved in protein and mtDNA quality control, was up-regulated at mRNA and protein levels under all conditions
(PDF) The Lon protease removes excess signal recognition particle - The Lon protease removes excess signal recognition particle protein in Escherichia coli ... suggesting that Ffh residue G405 is involved in ... severe depletion of either Ffh or the 4.5S RNA have
The Lon Protease Links Nucleotide Metabolism with Proteotoxic Stress - Abstract. During proteotoxic stress, bacteria maintain critical processes like DNA replication while removing misfolded proteins, which are degraded by the Lon protease. Here, we show that in Caulobacter crescentus Lon controls deoxyribonucleoside triphosphate (dNTP) pools during stress through degradation of the transcription factor CcrM
Highly Contingent Phenotypes of Lon Protease Deficiency in Escherichia - Drug concentration-dependent effects of Lon deficiency in E. coli challenged with trimethoprim.. In order to test how the Lon protease impacted the intrinsic susceptibility of E. coli to antibiotics, I created a Lon-deficient strain by replacing the lon gene with a kanamycin resistance cassette (here referred to as E. coli Δlon) (Fig. 1A).I then compared the dose-response characteristics of
Highly Contingent Phenotypes of Lon Protease Deficiency in ... - PubMed - Evolutionary trajectories and mutational landscapes of drug-resistant bacteria are influenced by cell-intrinsic and extrinsic factors. In this study, I demonstrated that loss of the Lon protease altered susceptibility of Escherichia coli to trimethoprim and that these effects were strongly contingent on the drug concentration and genetic background
Mitochondrial Lon protease - depleted HeLa cells exhibit proteome - The ATP-dependent Lon protease is located in the mitochondrial matrix and oxidized proteins are among its primary targets for their degradation. ... we now show that Lon knockdown leads to modifications of the expression of a number of specific proteins involved in protein quality control, stress response and energy metabolism, as evidenced
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- A deficiency of the Escherichia coli Lon protease blocked paradoxical survival occurring at very high nalidixic acid concentrations. The absence of Lon also blocked a parallel increase in cell lysate viscosity likely to reflect DNA size. Thus, Lon may participate in repairing quinolone-mediated DNA lesions formed at high drug concentrations
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Lon Protease Is Essential for Paradoxical Survival of - A deficiency of the Escherichia coli Lon protease blocked paradoxical survival occurring at very high nalidixic acid concentrations. The absence of Lon also blocked a parallel increase in cell
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- A deficiency of the Escherichia coli Lon protease blocked paradoxical survival occurring at very high nalidixic acid concentrations. The absence of Lon also blocked a parallel increase in cell lysate viscosity likely to reflect DNA size. Thus, Lon may participate in repairing quinolone-mediated DNA lesions formed at high drug concentrations
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An Integrated Proteomic Approach Uncovers Novel Substrates - Abstract Controlling the cellular abundance and proper function of proteins by proteolysis is a universal process in all living organisms. In Escherichia coli, the ATP-dependent Lon protease is crucial for protein quality control and regulatory processes
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Mitochondrial Lon protease is a gatekeeper for proteins newly ... - Nat… - What is the function of Lon protease?
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Mitochondrial Lon protease is a gatekeeper for proteins newly - The Lon proteases contain serine protease domains, whereas AFG3L2 and paraplegin belong to the metalloprotease family. Mutations in the gene encoding LONP1 cause cerebral, ocular, dental,
Lon Protease Is Essential for Paradoxical Survival of - A deficiency of the Escherichia coli Lon protease blocked paradoxical survival occurring at very high nalidixic acid concentrations. The absence of Lon also blocked a parallel increase in cell lysate viscosity likely to reflect DNA size. Thus, Lon may participate in repairing quinolone-mediated DNA lesions formed at high drug concentrations