Arabidopsis thaliana

Arabidopsis Mitochondria Leaf Proteome

Heat map of normalized intensity profiles of the proteins included in a mitochondrial fraction from Arabidopsis thaliana leaves. The map consists of 70 columns corresponding to the 70 gel slices and 1359 lines corresponding to the 1359 identified unique proteins. Relative protein quantity is indicated by shades of blue (dark blue stands for high quantity, light blue/white for low quantity). Quantitative profiles of proteins are aligned according to similarity by hierarchical clustering using the NOVA software.

Arabidopsis: Small + Large Ribosomal Cluster (lpBN Gel)

Abundance profiles of ribosomal and ribosome-related proteins in cross-linked Arabidopsis leaf mitochondria. Proteins of a mitochondrial fraction isolated from leaf material treated with formaldehyde immediately after cell disruption were solubilized with digitonin and separated by lpBN PAGE. The resulting gel lane was cut into 45 fractions and all fractions were subjected to label-free quantitative shotgun proteomics. The heatmap displays the abundance profiles of proteins annotated as ribosomal subunits or ribosome associated proteins detected in this approach. Please note that the clusters shown here do are different to the master heatmap containing all identified proteins due to the selection process. Protein abundance is illustrated by color: white is absence of detection, shades of blue indicate amounts relative to the highest detected abundance of a particular protein across all fractions.

Arabidopsis: Small Ribosomal Cluster (BN Gel)

Abundance profiles of small subunit ribosomal proteins and associated proteins in cross-linked Arabidopsis leaf mitochondria. Proteins of a mitochondrial fraction isolated from leaf material treated with formaldehyde immediately after cell disruption were solubilized with digitonin and separated by lpBN PAGE. The resulting gel lane was cut into 45 fractions and all fractions were subjected to label-free quantitative shotgun proteomics. Heatmap is a cutout of the master heatmap derived from hierarchical clustering of all identified proteins. Protein abundance is illustrated by color: white is absence of detection, shades of blue indicate amounts relative to the highest detected abundance of a particular protein across all fractions (dark blue).

Arabidopsis: Large Ribosomal Cluster (BN Gel)

Abundance profiles of large subunit ribosomal proteins and associated proteins in cross-linked Arabidopsis leaf mitochondria. Proteins of a mitochondrial fraction isolated from leaf material treated with formaldehyde immediately after cell disruption were solubilized with digitonin and separated by lpBN PAGE. The resulting gel lane was cut into 45 fractions and all fractions were subjected to label-free quantitative shotgun proteomics. Heatmap is a cutout of the master heatmap derived from hierarchical clustering of all identified proteins. Protein abundance is illustrated by color: white is absence of detection, shades of blue indicate amounts relative to the highest detected abundance of a particular protein across all fractions.

Arabidopsis: Small + Large Ribosomal Cluster (Sucrose Velocity Gradient)

Abundance profiles of small and large ribosomal subunits separated by sucrose velocity density gradient ultracentrifugation. Proteins of a mitochondrial fraction isolated from leaf material treated with formaldehyde immediately after cell disruption were solubilized with digitonin and separated in an 8% to 40% sucrose gradient. The gradient was divided into 29 fractions, each of which being subjected to label-free quantitative shotgun analysis. Hierarchical clustering of MS results yieldeda heatmap in the same fashion as outlined for the lpBN PAGE. Cutouts of the master clusters containing small subunit (top cluster) and large subunit (bottom cluster) are shown. Protein abundance is illustrated by color: white is absence of detection, shades of brown indicate amounts relative to the highest detected abundance of a particular protein across all fractions.

Imprint                   Author: Michael Senkler