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6,171 results for “mutant”
Ionome analysis of Salmonella mutants by Inductively coupled plasma mass spectrometry (ICP-MS)
<p>In many Gram-negative bacteria, the stress sigma factor of RNA polymerase, σS/RpoS, remodels global gene expression to reshape the physiology of quiescent cells and ensure their survival under non-optimal growth conditions. In the foodborne pathogen <i>Salmonella enterica</i> serovar Typhimurium, σS is also required for biofilm formation and virulence.</p><p>We have previously shown that a Δ<i>rpoS</i> mutation affects the <i>Salmonella</i> ionome. Indeed, inductively coupled plasma mass spectrometry analyses have unraveled a significant effect of the Δ<i>rpoS </i>mutation on the cellular concentration of manganese, magnesium, cobalt and potassium, suggesting that σS controls fluxes of ions that might be important for the fitness of quiescent cells (Metaane et al. 2022, PLoS ONE 17(3): e0265511).</p><p>Study: These findings prompted us to evaluate the impact on the<i> Salmonella</i> ionome of deletions of genes encoding the <i>Salmonella</i> Mn2+ transporters (<i>sitABCD</i> and <i>mntH</i>), the Co2+ transporter (<i>cbiMNQO</i> operon) and small proteins of unkown function (<i>yqaE</i> and <i>yqjDEK</i>) that accumulate in quiescent <i>Salmonella</i> under the tight control of σS (Levi-Meyrueis et al. PloS one. 2014; 9(5):e96918, Lago et al. Scientific reports. 2017; 7(1):2127 and Metaane et al. 2022, PLoS ONE 17(3): e0265511).</p><p>Material and Methods: Cell-associated contents of several elements were measured by inductively coupled plasma mass spectrometry (ICP-MS) as previously described in Metaane <i>et al </i>2022 PLoS ONE 17(3): e0265511.Dried cell pellets were prepared by V. Monteil and F. Norel (Institut Pasteur, Université de Paris, CNRS UMR3528, Biochimie des Interactions Macromoléculaires, F-75015, Paris, France). Cell-associated contents of several elements were measured by S. Ayrault and L. Bordier (ICP-MS platform, Laboratoire des Sciences du Climat et de l'Environnement, LSCE/IPSL, CEA-CNRSUVSQ,Université Paris-Saclay, 91191, Gif-sur-Yvette, France)</p><p><strong>This work was supported by the French National Research Agency (ANR-19-CE44-0005-01, PERIOMET project).</strong></p><p><strong>Linked studies:</strong></p><ul><li>NOREL Francoise, MONTEIL Veronique, DOUCHE Thibaut, & MATONDO Mariette. (2023). Global effects of deletions of the sitABCD, mntH, cbiMNQO and corA genes, encoding transporters for manganese, cobalt and magnesium on protein abundance in Salmonella enterica serovar Typhimurium grown to stationary phase in LB. [Data set]. Zenodo. https://doi.org/10.5281/zenodo.8279780</li><li>Metaane S, Monteil V, Douché T, Giai Gianetto Q, Matondo M, Maufrais C, Norel F. Loss of CorA, the primary magnesium transporter of <i>Salmonella, </i>is alleviated by MgtA and PhoP-dependent compensatory mechanisms. PloS one. 2023;18(9):e0291736.</li></ul>
Dataset of Molecular Dynamics Simulations for the Upregulated Biomarker PSMB8: 3UNF and its G210V Mutant in Experimental Autoimmune Encephalomyelitis
<p>This dataset contains molecular dynamics simulations data generated using GROMACS for the upregulated biomarker 3UNF and its G210V mutant in the context of Experimental Autoimmune Encephalomyelitis (EAE). EAE is a widely studied animal model for multiple sclerosis, and investigating the behavior of biomarkers in this model is crucial for understanding disease progression and potential therapeutic interventions.</p> <p>The dataset includes trajectory files, coordinate files, and relevant parameters used in the simulations. These simulations provide valuable insights into the structural dynamics, conformational changes, and interactions of the PSMB8 biomarker 3UNF and its G210V mutant within the EAE system. The data offers researchers an opportunity to analyze and explore the behavior of these biomarkers at the atomic level, aiding in the identification of potential binding partners, functional sites, and mechanisms associated with disease progression.</p> <p>By sharing this dataset, we aim to contribute to the scientific community by providing a valuable resource for further analysis, validation, and comparison of the molecular behavior of the upregulated biomarker 3UNF and its G210V mutant in Experimental Autoimmune Encephalomyelitis.</p>
QC and WGS data on compound heterozygous PRKN-mutant (R275W/dEx8) PD patient
<p>Primary/raw data for QC on the characterisation of an iPSC line from a PD patient (Stem Cell Research)</p>
Chemical-genetic interrogation of RNA polymerase mutants reveals structure-function relationships and physiological tradeoffs
<p>The multi-subunit bacterial RNA polymerase (RNAP) and its associated regulators carry out transcription and integrate myriad regulatory signals. Numerous studies have interrogated the inner workings of RNAP, and mutations in genes encoding RNAP drive adaptation of <i>Escherichia coli</i> to many health- and industry-relevant environments, yet a paucity of systematic analyses has hampered our understanding of the fitness benefits and trade-offs from altering RNAP function. Here, we conduct a chemical-genetic analysis of a library of RNAP mutants. We discover phenotypes for non-essential insertions, show that clustering mutant phenotypes increases their predictive power for drawing functional inferences, and demonstrate that some RNA polymerase mutants both decrease average cell length and confer insensitivity to killing by cell-wall targeting antibiotics. Our findings demonstrate that RNAP chemical-genetic interactions provide a general platform for interrogating structure-function relationships <i>in vivo</i> and for identifying physiological trade-offs of mutations, including those relevant for disease and biotechnology. This strategy should have broad utility for illuminating the role of other important protein complexes.</p>
Raw diffraction images of heliorhodopsin E108D mutant
<p>Crystal structure of <em>Thermoplasmatales archaeon</em> heliorhodopsin E108D mutant<em> </em>(PDB code: <a href="https://www.rcsb.org/structure/7CLJ">7CLJ</a>).</p> <p>79 small-wedge (10°/crystal) datasets collected from loop-harvested microcrystals using <a href="https://github.com/keitaroyam/yamtbx/blob/master/doc/eiger-en.md">EIGER</a> X 9M detector at a wavelength of 1 Å on BL32XU, SPring-8. Beam size was around 5×5 µm<sup>2</sup> and oscillation step was 0.1°. The crystals belonged to space group P4<sub>2</sub>2<sub>1</sub>2 with unit cell parameters a~72.9, c~115 Å.</p> <p>52 datasets were indexed and integrated using XDS with <a href="https://github.com/keitaroyam/yamtbx/blob/master/doc/kamo-en.md">KAMO</a> pipeline. Finally 12 integrated results were merged at 2.6 Å resolution after CC-based clustering and outlier rejection by KAMO in the published result (<a href="https://doi.org/10.1016/j.bbrc.2020.06.124">Tanaka et al. BBRC, 2020</a>).</p>
Cofactor specificity of the tetrameric 6-phosphogluconate dehydrogenase from Gluconobacter oxydans: Studies of wild-type and mutants forms.
<p>Here we present the results regarding the characterization of the kinetics parameters for NAD and NADP of the 6-phosphogluconate dehydrogenase from Gluconobacter oxydans at different concentrations of 6PG.</p> <p>The raw data of kinetic parameters for NAD or NADP at different 6PG concentrations are represented in kcat and KM, with the units s-1 and µM, respectively. Al the rest values as an efficient constant are represented in s-1µM-1. </p> <p>Also, we included the kinetic characterizations of the mutants Go6PGDH-R31L, Go6PGDH-R31V, and Go6PGDH-D30N. The CSV files contain four columns. 1. NAD or NADP concentration in µM; 2. enzyme activity in U/mg; 3. Standard deviation and 4. The number of independent experiments. </p> <p> </p> <p> </p> <p> </p>
Competitive growth experiments with a high-lipid Chlamydomonas reinhardtii mutant strain and its wild-type to predict industrial and ecological risks
<p>Key microalgal species are currently being exploited as biomanufacturing platforms using mass cultivation systems. The opportunities to enhance productivity levels or produce non-native compounds are increasing as genetic manipulation and metabolic engineering tools are rapidly advancing. Regardless of the end product, there are both environmental and industrial risks associated to open pond cultivation of mutant microalgal strains. A mutant escape could be detrimental to local biodiversity and increase the risk of algal blooms. Similarly, if the cultivation pond is invaded by a wild-type microalgae or the mutant reverts to wild-type phenotypes, productivity could be impacted. To investigate these potential risks, a response surface methodology was applied to determine the competitive outcome of two <em>Chlamydomonas reinhardtii</em> strains, a wild-type (CC-124) and a high-lipid accumulating mutant (CC-4333), grown in mixotrophic conditions, with differing levels of nitrogen and initial wild-type to mutant ratios. Results of the growth experiments show that mutant cells have double the exponential growth rate of the wild-type in monoculture. However, due to a slower transition from lag phase to exponential phase, mutant cells are outcompeted by the wild-type in every co-culture treatment. This suggests that, under the conditions tested, outdoor cultivation of the <em>C. reinhardtii</em> cell wall-deficient mutant strains does not carry a significant environmental risk to its wild-type in an escape scenario. Furthermore, lipid results show the mutant strain accumulates over 200% more TAGs per cell, at 50 mg/L NH<sub>4</sub>Cl, compared to the wild-type, therefore, the fragility of the mutant strain could impact on overall industrial productivity.</p>
X-ray diffraction images for the H145E mutant of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis.
<p>X-ray diffraction images of the H145E mutant (prefixed h145e) which were collected in October 1995 using a graphite-monochromated copper K-alpha rotating anode source (wavelength 1.5418 Å) with a Marresearch 90 cm image plate detector at a distance of 120 mm from the crystal. The data were collected at room temperature in two passes, each consisting of 100 one degree rotations of the crystal. Each image had an exposure time of 20 minutes. The crystal was rotated in the capillary tube prior to collection of the second pass in order to record the 'blind' region of the diffraction pattern and this set of images is prefixed h145eb. </p>
X-ray diffraction images for the H145Q mutant of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis.
<p>X-ray diffraction images collected from one crystal at room temperature using a rotating anode copper source (wavelength 1.5418 Å) and a 30 cm Marresearch image plate detector. The crystal-to-detector distance was 150 mm and a 90 mm image plate scan radius was used. Each of the 60 images had an exposure time of 20 minutes and corresponds to a 3 degree phi-rotation of the crystal. Diffraction extends to about 3.3 Å resolution. </p>
Molecular dynamic trajectory of calcium binding T163S mutant for the article "Ca 2+ binding to F-ATP synthase β subunit triggers the mitochondrial permeability transition"
<p>ATP synthase molecular dynamics simulations files for T163S mutants of the beta subunit binding calcium:</p> <p>50ns trajectory (ATPsynth_woh2o_Ca_mut.dcd) and corresponding psf file (ATPsynth_ca_mut.psf)</p>
Molecular dynamic trajectory of magnesium binding T163S mutant for the article "Ca 2+ binding to F-ATP synthase β subunit triggers the mitochondrial permeability transition"
<p>ATP synthase molecular dynamics simulations files for T163S mutants of the beta subunit binding magnesium:</p> <p>50ns trajectory (ATPsynth_woh2o_Mg_mut.dcd) and corresponding psf file (ATPsynth_mg_mut.psf)</p> <p> </p>
Effect of shade and nitrogen content on Arabidopsis Col-0 and cytokinin mutants abcg14 and cypDM mRNA-seq gene expression processed tables.
<p>This dataset is an add-on for Gautrat et al., containing processed files for the mRNAseq data in tab delimited txt format.</p> <p>Here, you can obtain the raw counts file, the normalized CPM values, and the normalized logCPM values</p> <p>The RNA-seq raw data supporting the conclusions of this article have been deposited in ArrayExpress (Kolesnikov et al., 2015) at EMBL-EBI (www.ebi.ac.uk/arrayexpress), under accession numbers E-MTAB-13638.</p> <p>All relevant custom r scripts are available at https://github.com/aromanowski/shade_N_ck</p>
Computational Insights into the Unfolding of a Destabilized Superoxide Dismutase 1 Mutant
<p>This data accompanies the article entitled <em>Computational Insights into the Unfolding of a Destabilized Superoxide Dismutase 1 Mutant</em> and published in Biology.</p> <p>SOD1_WT_I35A_REST2.zip: The zip archive includes REST2 trajectories for the two SOD1 constructs and the two force fields investigated in the paper.</p> <p>The trajectories are saved in the GROMACS XTC file format, separately for each temperature (i=0,...,23). Owing to the considerable trajectory sizes, only protein coordinates are reported, and the output frequency is reduced to 100 ps. The initial geometry (in the Gromos87 GRO format) after a short relaxation is provided for each REST2 simulation (conf_prot.gro). Furthermore, for each REST2 simulation, an xarray (http://xarray.pydata.org) dataset, saved in the netCDF file format, is included and contains the following observables: fraction of native contacts relative to the crystal structure, secondary-structure content (i.e., the fraction of protein residues found in an alpha-helix, beta-sheet, beta-bridge, or a turn), as well as the number of residues with the beta-sheet secondary structure per each beta-strand and beta-sheet of the SOD1 barrel.</p>
Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) mutant G258A (PDB entry 7AAL)
<p>Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (residues 1-289), mutant G258A.</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.9999 Å wavelength and a PILATUS3 6M detector. The dataset consists of 2400 images (0.15 degree oscillation per image). Crystals belong to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.19 Å, b=73.02 Å, c=205.25 Å. The asymmetric unit contains an homodimer of the F-BAR domain (~53% solvent content), which is the biological unit.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 2.92 Å in the direction b* and the highest limits were 1.97 Å and 2.09 in the directions a* and c*, respectively.</p> <p> </p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Martín, V. Casas J, Alcón P, Sánchez Crespo M, Bayón Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code 7AAL:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aal">https://www.ebi.ac.uk/pdbe/entry/pdb/7aal</a></p>
Molecular dynamics simulation trajectories of HIV protein gp120 in complex with antibody VRC01 and 30 of its Ala mutants
<p>This data set accompanies the publication by S. Conti, E. Lau, and V. Ovchinnikov entitled "On the rapid calculation of binding affinities for antigen and antibody design and affinity maturation simulations", to be published in the MDPI journal Antibodies. It contains molecular dynamics simulation trajectories of HIV protein gp120 in complex with antibody VRC01 and 30 of its Ala mutants, as described in the paper. The format of the trajectory files is CHARMM-compatible dcd. The files can be visualized with the program Visual Molecular Dynamics (VMD) (see paper by Humphrey et al. 1996, J. Molec. Graphics). The accompanying file "view" is a tcl-based script for VMD that can be executed in the Linux environment using: "vmd -e view", which will display the trajectory of the mutant specified by editing the first noncomment line of the script.<br> </p>
Diffraction images of a crystal of the complex formed by fragments of the integrin beta4 and the bullous pemphigoid antigen 1 (BP230, BPAG1e). Integrin high affinity point mutant. PDB entry 6GVK.
<p>Data were collected on a single crystal at the beamline XALOC of the ALBA-CELLS synchrotron facility (Cerdanyola del Vallés, Barcelona, Spain) using radiation of 0.97915 Å wavelength and a PILATUS 6M detector. The complete dataset is build up of three sub-sets measured at three different positions of a single crystal. Each sub-set consists of 1800 images (0.2 degree oscillation per image).</p>
Enrichment of gene sets altered in dram1 mutant zebrafish larvae
<p>Enrichment of gene sets altered in dram1 mutant zebrafish larvae.</p> <p>A. Gene Ontology categories significantly over and underrepresented in the significant genes differentially regulated between <em>dram1</em><sup>∆19n/∆19n </sup>PBS-injected mutants compared to <em>dram1</em><sup>+/+</sup> larvae.</p> <p>B. Gene sets from the MSigDB C2 database significantly positively correlated to the <em>dram1</em><sup>∆19n/∆19n </sup>mutants transcriptome compared to <em>dram1</em><sup>+/+</sup> larvae.</p> <p>C. Gene sets from the MSigDB C2 database significantly negatively correlated to the <em>dram1</em><sup>∆19n/∆19n </sup>mutants transcriptome compared to <em>dram1</em><sup>+/+</sup> larvae.</p>
Seminal Root Images of Wheat TILLING Mutants
<p>These files describe a forward genetic screen for variation in seminal root traits in a subset of an exome-sequenced wheat TILLING population in the UK bread wheat cultivar - Cadenza. The submission contains:</p> <ol> <li>readme.md: Contains detailed description of the dataset and experiment.</li> <li>List_of_Lines_Phenotyped.csv: Contains a list of the subset of the Cadenza TILLING population phenotyped.</li> <li>Cadenza_TILLING_Mutants_RootNav_Measurement.csv: Contains the original root trait measurements from RootNav (Root image analysis software).</li> <li>Wheat_TILLING_Seminal_Root_Images.tar.gz: An archive containing 6,240 root images of the mutant lines and control phenotyped.<br> </li> </ol>
Antiviral activity of HIV-1 integrase strand-transfer inhibitors against mutants with integrase resistance-associated mutations and their frequency in treatment-naïve individuals
<p>The development of resistance to human immunodeficiency virus 1 (HIV-1) integrase strand-transfer inhibitors (INSTI) has been documented; however, knowledge of the impact of pre-existing integrase (IN) mutations on INSTI resistance (INSTI-R) is still evolving. The frequency of HIV-1 IN mutations in 2177 treatment-naïve subjects was investigated, along with the INSTI susceptibility of site-directed mutant viruses containing major and minor INSTI-R mutations. Total 6 of 39 minor INSTI-R mutations (M50I, S119P/G/T/R, and E157Q) were found in >1% of IN-treatment-naïve subjects with no impact on INSTI susceptibility. When each combined with major INSTI-R mutation, M50I, S119P, and E157Q led to decreased susceptibility to elvitegravir but remained sensitive to dolutegravir and bictegravir.</p>
Representative snapshots of imaging sequences used in transcan_IDH-mutant_LGG_radiomics analysis
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International Brain Laboratory public data
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OpenNeuro
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