GWJ-NUI-MAY · Identification of potential prion proteins in plants
6РП — Действия „Мария Кюри“
- Период
- 2005-03-01 → 2007-02-28
- Финансиране от ЕС
- 80 000 €
- Участници
- 1
- Схема
- IRG
Линиите свързват координатора с партньорите.
Накратко на български
Прионните протеини при растенията, като тези при Arabidopsis thaliana, се търсят чрез тестове с дрожди. Това помага да се разбере нов механизъм за промяна на функциите на протеините и еволюцията на протеините-шаперони.
Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.
Резултати накратко
Final Activity Report Summary - GWJ-NUI-MAY (Identification of potential prion proteins in plants)
The main aim of this project was to identify new prion proteins in plants. Recent work from various diverse species suggests that the term prion should not only be associated with diseases such as 'Mad cow disease' etc, but should be used as a general term for any protein that can behave in an infectious manner. This suggestion has far- reaching implications for many aspects of biological processes. This project set out to apply what we know characterises a prion protein in Saccharomyces cerevisiae (baker's yeast) to try and identify potential prion- forming proteins in the model plant Arabidopsis thaliana. To this end we have identified two plant proteins that have the ability to form prions in a yeast system. The next and most challenging aspect is to establish whether these proteins can form prions in their natural environments. The pint must be emphasised, these potential prion proteins in plants are unrelated to human disease and potentially constitute a new mechanism in plants for altering protein function. In addition to searching for new prion proteins, this project has also assessed the ability of plant chaperone proteins (to function correctly in yeast. A chaperone is a protein that helps other proteins to obtain their proper 3 dimensional structure- they are implicated in a number of human disease states) These experiments have helped address questions regarding the evolution of the Hsp70 protein (a major class of protein chaperone).
Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз
Цел на проекта
This proposal seeks to identify potential prion proteins within the model plant Arabidopsis thaliana.The term prion was first used to describe the infectious agent causing scrapie, a transmissiblespongiform encephalopathy (TSE) disease, in sheep. Since the n TSE's have been identified in cattle (BSE) and an association between BSE and a variant of a human TSE, Cruetzfeld-Jakob disease (CJD),have been established. The identification of prion-like proteins in Saccharomyces cerevisiae has opened up a new era in t he study of prion proteins.As well as redefining the term prion to encompass an array of proteins that can behave in an infectious manner, the discovery of prions in yeast allows detailed genetic analysis to be carried out on factors affecting prion stability and propagation using well-established yeast genetic techniques. Furthermore, studies of yeast prions suggest that the prion phenomena may well be widespread throughout nature and that prions have the ability to carry out normal cellular functions. Prionisation domains have been identified and have been shown to be transferable. Using bio-informatics techniques a number of plant proteins that contain putative prion domains have identified. The experimental approach to be taken in this proposal is to transfer these potential plant prion domains and fuse them with green fluorescent protein (GFP) and also use them to replace the prion domain of the known yeast prion protein Sup35. Prions in yeast form aggregates.We will therefore monitor the aggregation state of GF P in the constructs and observe if they behave like known yeast prions. We will also carry out detailed yeast genetics to investigate whether the plant prion domains can substitute for the natural prion domain of the Sup35 protein. In addition, we will create and screen an Arabidopsis prion domain library constructed from random plant amino acid sequences fused to a yeast selectable marker. Yeast
Оригинален текст от CORDIS (на английски).
Участници
- National University of Ireland - Maynooth · MAYNOOTHКоординаторИрландия
Връзки
Данни: CORDIS, © Европейски съюз