SACP · Role of Senescence-associated Cysteine Proteases
7РП — „Хора“ (Действия „Мария Кюри“)
- Период
- 2010-03-01 → 2010-11-30
- Финансиране от ЕС
- 160 997 €
- Участници
- 1
- Схема
- MC-IEF
Линиите свързват координатора с партньорите.
Накратко на български
Ензимите, които разграждат протеини при стареенето на листата при растенията (например при Arabidopsis), се проучват чрез специални сонди. Това помага да се разбере как се разгражда Рубиско – най-разпространеният протеин в света.
Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.
Резултати накратко
Role of Senescence-associated Cysteine Proteases
Project objectives The aim of the project was to identify proteases that are responsible for leaf senescence in plants, which involves a massive degradation of rubisco, the most abundant protein in the world. Remarkably, the proteases involved in this proteolytic process are not yet known. The approach was to use activity-based profiling with probes for proteases to identify the protease activities that are up-regulated during leaf senescence in Arabidopsis, and subsequently to address their role in senescence using reverse genetic approaches. Probes for the proteasome, serine proteases and vacuolar processing enzymes did not reveal significantly increased activities of any of these enzymes during senescence. In contrast, probes for papain-like cysteine proteases showed an increased activity of some of these enzymes during senescence, predominantly caused by increased levels of one protease called RD21. Additional senescence-related proteases identified by mass spectrometry included SAG12, which is used as a transcriptional marker for senescence. Surprisingly, Arabidopsis mutants lacking RD21 or other senescence-related proteases did not have phenotypes in senescence assays, such as chlorophyll degradation, despite the fact that they have significantly reduced protease activities in senescing leaves. These data suggest that these proteases act redundantly with other senescence-related proteases. Further work would therefore require the generation and analysis of double and triple knockout lines. The project ran for eight months in Cologne with MC-IEF funding and is being continued by the fellow outside Europe with different funding.
Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз
Цел на проекта
Despite the importance of senescence in world food production and safety, the proteases responsible for the massive protein degradation during senescence have not been identified. Strong candidates for senescence-associated proteases are members of various cysteine protease families that localize in lytic vacuoles that presumably engulf the chloroplast during senescence. This project aims at identifying the proteases that degrade chloroplasts in the model plant Arabidopsis thaliana. To detect and identify the active proteases during senescence the Activity-based Protease Profiling (ABPP) will be applied. ABPP is a novel functional proteomics technology based on the use of labeled small molecule inhibitors that label proteases in an activity-dependent manner. This technology can be used to show where, when and which proteases are active during senescence, and will reveal proteases that act redundantly. The role of these proteases in senescence will be further studied using reverse genetics and cell biological approaches. This project extends on the expertise and interest of the applicant in senescence and provides an excellent interdisciplinary training in cell biology, molecular cloning and state-of-the-art chemical biology. By performing this work in the Plant Chemetics lab at the Max Planck institute for Plant Breeding Research in Cologne, the applicant will have access to one of the best research and training facilities in Europe and leave at the end of the project with the knowledge and materials to establish an independent scientific career.
Оригинален текст от CORDIS (на английски).
Участници
- MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV · MUNCHENКоординаторГермания
Връзки
Данни: CORDIS, © Европейски съюз
