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CHARACTERIZATION OF A NOVEL CHLOROPLAST PROTEASE |
| Host Laboratory | Scientific Supervisor | |
| Hebrew University of Jerusalem The Authority for Research and Development Department of Agricultural Botany - Faculty of Agriculture P.O.BOX 12 76100 Rehovot Israel |
Dr. Zach Adam Tel : 972/89481329 / Fax : 972/89467763 Email : zach@agri.huji.ac.il | |
| Grant Holder | ||
| MADAME Marika Lindahl (Sweden) Tel : 46/8163148 / Fax : 46/8153679 | ||
| Abstract Research objectives and content The components of the phytosynthesis apparatus and the associated reactions are known in molecular detail. In contrast, the mechanisms of regulation of these processes and the enzymes responsible are largely unknown. Associated with the utilization of light as a substrate and with the high oxidizing potential created during photosynthesis is a unique set of problems due to the damage caused to the proteins involved. Damaged proteins are currently degraded and replaced by newly synthesised copies. Despite the numerous proteolytic events described, none of the proteases have hitherto been identified. We have previously demonstrated the presence of a putative protease, homologous to the bacterial FtsH protease, which is integral to the thylakoid membrane in a position which renders it an excellent candidate for an enzyme responsible for regulatory proteolysis during chloroplast biogenesis and maintenance. The planned research involves detailed characterization of this FtsH like protease aimed at establishment of its role in chloroplast function. Thus, we expect to considerably advance the understanding of chloroplast proteolytic mechanisms. Training content (objective, benefit and expected impact) During my PhD studies I have focused on the biochemical aspects of chloroplast biology. My present work involves purification of soluble as well as membrane bound proteins and characterization of their enzymatic activities. Therefore, it will be highly valuable for me to learn the methods and concepts of molecular biology in order to acquire a wider competence in my own scientific area. The research project and the laboratory of choice offer a number of possibilities to perform molecular cloning, site-directed mutagenesis and over-expression of chloroplast genes in E. coli. Links with industry / industrial relevance (22) Contract number : FMBICT972386 | ||
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