Several fully disordered proteins have been reported to show chaperone activity under environmental stress conditions, without the exact understanding of the mechanism. Some of these proteins belong to late embryogenesis abundant (LEA) proteins of plants and being expressed in the plant during the late stage of seed development and under cold or dehydration stress conditions. In vitro and in vivo studies have revealed several biochemical functions of these proteins that are unambiguous in the physiology of the plant, among which one is the chaperone activity. Whereas the physiological role of these chaperone proteins is clear, neither their physiological partners nor the molecular mechanism are known.
ERD14, a member of the LEA family in A. thaliana has evidence to possess potent chaperone activity in vitro. To provide an in depth analysis of the molecular mechanism of the fully disordered chaperone ERD14, both in vitro and in vivo, we have designed and integrated experimental strategy to answer these questions. First, by finding physiological substrates and describing the chaperone mechanism in vitro, and later in vivo using in cell NMR. To support these experimental approaches and also to investigate the chaperone behavior in the plant we have generated knock-out plants, and plants that are either overexpressing ERD14 or expressing a tagged version of the protein to have phenotypical information and also to investigate the behavior of the protein inside intact plant organism.
Original languageEnglish
Title of host publicationGordon Research Conference, Intrinsically disordered proteins (USA Vermont, 08.07.2012-13.07.2012) presented as a poster
Publication statusPublished - 8 Jul 2012
EventGordon Research Conference, Intrinsically disordered proteins - West Dover, VT, United States
Duration: 8 Jul 201213 Jul 2012

Conference

ConferenceGordon Research Conference, Intrinsically disordered proteins
CountryUnited States
CityWest Dover, VT
Period8/07/1213/07/12

    Research areas

  • Instrinsically disordered protein, Chaperones, Protein function

ID: 2531852