La Croix du Nord : supplément régional à la Croix de Paris ["puis" grand journal quotidien du Nord de la France]

17 novembre 19101910/11/17 (A21,N7320).Appartient à l’ensemble documentaire : NordPdeC

Expression pattern of LBPGs coexpressed genes.

<p>The module eigengenes are used to represent the genes expression pattern within each module. Each bar represents one sample (days after pollination) and the color represents the module color, the LBPGs was list below the module name. The value of the module eigengenes for each sample is displayed on the y axis.</p

Lysine biosynthesis pathway enzyme genes in maize.

<p>Lysine biosynthesis pathway enzyme genes in maize.</p

Regulation of LBPGs for maize seed Lysine biosynthesis.

<p>Regulation of LBPGs for maize seed Lysine biosynthesis.</p

Additional file 7. of Global analysis of uncapped mRNA changes under drought stress and microRNA-dependent endonucleolytic cleavages in foxtail millet

miRNA/target interactions identified in the degradome library by PAREsnip and function annotations of targets. Annotations were retrieved from phytozome. Note: Columns are blank if no corresponding data is available. (XLSX 40 kb

The motifs enriched in the LBPGs modules.

<p>The motifs enriched in 1-kb upstream sequences of the transcription start site of the LBPGs coexpressed module genes. (P-value was calculated by Ranksum test).</p

Phylogenetic trees of lysine biosynthesis pathway gene orthologs.

<p>Phylogenetic trees based on AK (aspartate kinase), ASD (aspartate-semialdehyde dehydrogenase), DHDPS (dihydrodipicolinate synthase), DapB (dihydrodipicolinate reductase), LL-DAP-AT (LL-diaminopimelate aminotransferase), DapF (diaminopimelate epimerase), and LysA (diaminopimelate decarboxylase) are shown. The AK tree contains two enzymes: the monofunctional enzyme AK (EC: 2.7.2.4; red branch) and the bifunctional enzyme HSDH (EC: 1.1.1.3; black branch)</p

Comparison of lysine content.

<p>(A) Comparison of lysine biosynthesis pathway genes coexpressed genes (LBPGs) with the same number of randomly selected all genes set (Test) and with all genes set (All). (B) Comparison of DHDPS1-coexpressed genes (DHDPS1) and DHDPS2-coexpressed genes (DHDPS2) with all genes set (All). (** <i>P</i> < 0.01)</p

Expression patterns of dihydrodipicolinate synthase (DHDPS) genes.

<p>(A) Expression levels reads per kilobase per million reads (RPKM) of DHDPS genes in 21 maize developmental stages. (B) Quantitative real-time PCR (qRT-PCR) validation of RNA-Seq-based DHDPS expression levels. qRT-PCR expression profiles (blue bars) of DHDPS genes closely match the RNA-Seq data (red lines). The correlation value (cor) was calculated using Pearson’s correlation coefficient. The error bars in the figure represent the standard deviation. (C) Heat map of expression profiles of DHDPS-coexpressed genes (Y axes). Numbers next to the heat map represent the number of days after pollination. (The error bars represent standard deviation).</p

Characterization and Functional Analysis of the Potato Pollen-Specific Microtubule-Associated Protein SBgLR in Tobacco

<div><p>Microtubule-associated proteins play a crucial role in the regulation of microtubule dynamics, and are very important for plant cell and organ development. SBgLR is a potato pollen-specific protein, with five imperfect V-V-E-K-K-N/E-E repetitive motifs that are responsible for microtubule binding activity. In present study, SBgLR showed typical microtubule-associated protein characteristics; it bound tubulin and microtubules, and colocalized with microtubules <i>in vitro</i>. We also found that SBgLR could form oligomers, and that both the SBgLR monomers and oligomers bundle microtubules <i>in vitro</i>. Constitutive expression of SBgLR in tobacco caused curving and right-handed twisting root growth, abnormal directional cell expansion and cell layer arrangement, and pollen abortion. Immunofluorescence staining assays revealed that microtubule organization is altered in root epidermal cells in SBgLR-overexpressing lines. These suggest that SBgLR functions as a microtubule-associated protein in pollen development. Our results indicate that normal organization of MTs may be crucial for pollen development.</p> </div