proteomics (מקור פרסום)
Rosen, R., Dept. of Molec. Microbiol./Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel, Institut für Mikrobiologie, Ernst-Moritz-Arndt-Univ. Greifswald, Germany
Sacher, A., Maiman Inst. for Proteome Research, George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Shechter, N., Dept. of Molec. Microbiol./Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Becher, D., Institut für Mikrobiologie, Ernst-Moritz-Arndt-Univ. Greifswald, Germany
Büttner, K., Institut für Mikrobiologie, Ernst-Moritz-Arndt-Univ. Greifswald, Germany
Biran, D., Dept. of Molec. Microbiol./Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Hecker, M., Institut für Mikrobiologie, Ernst-Moritz-Arndt-Univ. Greifswald, Germany
Ron, E.Z., Dept. of Molec. Microbiol./Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Proteomics based on two-dimensional (2-D) gel electrophoresis of proteins followed by spot identification with mass spectrometry is a commonly used method for physiological studies. Physiological proteomics requires 2-D reference maps, on which most of the main proteins are identified. We present a reference map for the bacterial plant pathogen Agrobacterium tumefaciens proteins, which contains more than 300 entries with an isoelectric point (p/) between 4 and 7. The quantitative study of the proteins in the analytical window of the master gel demonstrated unique features, in comparison with other bacteria. In addition, a theoretical analysis of several protein parameters was performed and compared with the experimental results. A comparison of the theoretical molecular weight (MW) of the proteins and their theoretical p/ with their vertical and horizontal migration distances, respectively, pointed out the existence of several proteins that strongly diverted from the graph trend-line. These proteins were clearly subjected to post-translational modifications, which changed their p/ and/or MW. Additional support for post-translational modifications comes from the identification of multiple spots of the same gene products. Post-translational modifications appear to be more common than expected, at least for soluble proteins, as more than 10% of the proteins were associated with multiple spots.
פותח על ידי קלירמאש פתרונות בע"מ -
הספר "אוצר וולקני"
אודות
תנאי שימוש
Two-dimensional reference map of Agrobacterium tumefaciens proteins
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Rosen, R., Dept. of Molec. Microbiol./Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel, Institut für Mikrobiologie, Ernst-Moritz-Arndt-Univ. Greifswald, Germany
Sacher, A., Maiman Inst. for Proteome Research, George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Shechter, N., Dept. of Molec. Microbiol./Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Becher, D., Institut für Mikrobiologie, Ernst-Moritz-Arndt-Univ. Greifswald, Germany
Büttner, K., Institut für Mikrobiologie, Ernst-Moritz-Arndt-Univ. Greifswald, Germany
Biran, D., Dept. of Molec. Microbiol./Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Hecker, M., Institut für Mikrobiologie, Ernst-Moritz-Arndt-Univ. Greifswald, Germany
Ron, E.Z., Dept. of Molec. Microbiol./Biotech., George S. Wise Fac. of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Two-dimensional reference map of Agrobacterium tumefaciens proteins
Proteomics based on two-dimensional (2-D) gel electrophoresis of proteins followed by spot identification with mass spectrometry is a commonly used method for physiological studies. Physiological proteomics requires 2-D reference maps, on which most of the main proteins are identified. We present a reference map for the bacterial plant pathogen Agrobacterium tumefaciens proteins, which contains more than 300 entries with an isoelectric point (p/) between 4 and 7. The quantitative study of the proteins in the analytical window of the master gel demonstrated unique features, in comparison with other bacteria. In addition, a theoretical analysis of several protein parameters was performed and compared with the experimental results. A comparison of the theoretical molecular weight (MW) of the proteins and their theoretical p/ with their vertical and horizontal migration distances, respectively, pointed out the existence of several proteins that strongly diverted from the graph trend-line. These proteins were clearly subjected to post-translational modifications, which changed their p/ and/or MW. Additional support for post-translational modifications comes from the identification of multiple spots of the same gene products. Post-translational modifications appear to be more common than expected, at least for soluble proteins, as more than 10% of the proteins were associated with multiple spots.
Scientific Publication