11 research outputs found

    Effects of TORC1 activity on magnetization.

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    <p>(A)Wild type harboring empty plasmid (Wild type), harboring multi-copy TCO89 plasmid (Multi-<i>TCO89</i>), and <i>tco89Δ</i> harboring empty plasmid (<i>tco89Δ</i>) were grown in selection medium containing 10 mM ferric citrate and 10 nM (red column), 20 nM (green column) rapamycin, or 0.2% dimethyl sulfoxide (DMSO) (blue column) as control. (B) Wild type (blue column) and <i>tco89Δ</i> (red column) are pre-cultured in synthetic complete medium and grown in indicated media containing 10 mM ferric citrate. Indications of media are synthetic complete medium containing 2% or 3% glucose (2% Glu, 3%Glu), 2- or 3-fold concentration of amino acid supplements (2×N, 3×N), or rich medium containing 2%, 3%, or 4% glucose (2% Glu, 3%Glu, and 4%Glu), respectively. Magnetization was measured as in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1001269#pbio-1001269-g003" target="_blank">Figure 3B</a>.</p

    Electron micrographs of magnetized cell.

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    <p>Normally grown cells (A–D) and iron-supplemented cells (E–T) of wild-type (A, E, I, M, and Q), ferritin-expressor (B, F, J, N, and R), <i>ccc1Δ</i> (C, G, K, O, and S), and <i>ccc1Δ</i> ferritin-expressor (D, H, L, P, and T) are shown. (M–P) 3× magnification of (I–L), respectively. Unstained sections are shown in (Q–T). Arrows indicate electron-dense particles. Scale bar, 500 nm.</p

    Magnetizable column entrapment.

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    <p>(A) Wild type cells grown in normal medium (Normal) and in 20 mM ferric citrate (iron supplemented) were applied to magnetizable column, and fractions of flow-through (Flow), wash-out (Wash), and trapped cells released after magnet detachment (Released) were collected and monitored by OD<sup>600</sup>. (B) Magnetic entrapment efficiency of the four strains. Percentages of trapped cells were calculated; mean ± s.d. (<i>n</i> = 3).</p

    Magnetization of yeast.

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    <p>(A) Iron tolerance affected by <i>ccc1Δ</i>, ferritin, and Fe<sup>2+</sup>/Fe<sup>3+</sup>. Culture of 2.0 OD<sup>600</sup> was diluted 10<sup>2</sup>, 10<sup>3</sup>, 10<sup>4</sup>, and 10<sup>5</sup>-fold in water, spotted by 10 ul from left to right for each strain, and grown on indicated plates. Empty, single-copy empty plasmid-harboring strain; Ferritin, single-copy ferritin gene set plasmid-harboring strain; Multi-empty, multi-copy empty plasmid-harboring strain; Multi-ferritin, multi-copy ferritin gene set plasmid-harboring strain. (B) Cell attraction towards magnet. Cell suspensions were placed over magnets (4×4 gray circles) and a picture taken at indicated times. Corresponding video is <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1001269#pbio.1001269.s003" target="_blank">Video S1</a>. (C) SQUID magnetization curve. Induced specific magnetic moment was measured as a function of applied magnetic field. Lines for the four strains without ferric citrate supplementation (No iron supplement) are almost identical and overlapped; mean ± s.d. (<i>n</i> = 3).</p

    Redox control by <i>TCO89</i>.

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    <p>(A) Dose-dependent effect of <i>TCO89</i> on cell redox state. Culture of 2.0 OD<sup>600</sup> was diluted 10<sup>2</sup>, 10<sup>3</sup>, 10<sup>4</sup>, and 10<sup>5</sup>-fold in water, spotted by 10 ul from left to right for each strain, and grown on indicated plates for 2 d, and colony staining by methylene blue was observed. Bluer color indicates more oxidized. (B) Cellular NADP measurement. NADP<sup>+</sup> (red column) and NADPH (blue column) were extracted from cells grown in liquid medium, measured, normalized by cell number, and plotted; mean ± s.d. (<i>n</i> = 3).</p

    Mass magnetic susceptibility of ferric citrate–supplemented cells.

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    <p>Mass magnetic susceptibility of ferric citrate–supplemented cells.</p

    MOESM1 of Genetic and physiological basis for antibody production by Kluyveromyces marxianus

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    Additional file 1: Table S1. Primers used in this study. Figure S1. Amino acid sequence of scFv. Figure S2. Sequence of codon optimized scFv fragment. Figure S3. Sequence of E02-014 plasmid. Figure S4. Sequence of KmPMDH1. Figure S5. Sequence of KmPACO1. Figure S6. Secreted scFv activity per cell amount

    A 100%-complete sequence reveals unusually simple genomic features in the hot-spring red alga -0

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    <p><b>Copyright information:</b></p><p>Taken from "A 100%-complete sequence reveals unusually simple genomic features in the hot-spring red alga "</p><p>http://www.biomedcentral.com/1741-7007/5/28</p><p>BMC Biology 2007;5():28-28.</p><p>Published online 10 Jul 2007</p><p>PMCID:PMC1955436.</p><p></p>e repeats, the histone cluster area, localization of transposable elements ('Class I' and 'Class II') and putative centromeric regions [9]

    A 100%-complete sequence reveals unusually simple genomic features in the hot-spring red alga -1

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    <p><b>Copyright information:</b></p><p>Taken from "A 100%-complete sequence reveals unusually simple genomic features in the hot-spring red alga "</p><p>http://www.biomedcentral.com/1741-7007/5/28</p><p>BMC Biology 2007;5():28-28.</p><p>Published online 10 Jul 2007</p><p>PMCID:PMC1955436.</p><p></p>ively. H4-a, histone H4-a; H2B-a, histone H2B-a; ADF, actin-depolymerizing factor; S/TPK, RIO-like serine/threonine protein kinase; 40S-S13, 40S ribosomal protein S13; H3-b, histone H3-b; PTR, possible transcribed region; H2A-b, histone H2A-b; H3-c, histone H3-c; TIM50, mitochondrial preseqence translocase subunit Tim50; BAT, brabched-chain-amino-acid transaminase, mitochondrial precursor; H1, histone H1; ASM, similar to N6-adenine-specific methylase; Hyp, hypothetical transcript; TPR, hypothetical protein, conserved (containing tetratricopeptide repeats); CAB-CP24, similar to chlorophyll a/b-binding protein, CP24; H2B-b, histone H2B-b; Hyp, hypothetical protein; H4-b, histone H4-b

    A 100%-complete sequence reveals unusually simple genomic features in the hot-spring red alga -3

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    <p><b>Copyright information:</b></p><p>Taken from "A 100%-complete sequence reveals unusually simple genomic features in the hot-spring red alga "</p><p>http://www.biomedcentral.com/1741-7007/5/28</p><p>BMC Biology 2007;5():28-28.</p><p>Published online 10 Jul 2007</p><p>PMCID:PMC1955436.</p><p></p>e repeats, the histone cluster area, localization of transposable elements ('Class I' and 'Class II') and putative centromeric regions [9]
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