Structural flexibility of a recombinant intrinsically disordered LEA protein from Ramonda serbica.

ABSTRACT: Late embryogenesis abundant (LEA) proteins play a crucial role in the desiccation tolerance of resurrection plants, although their exact functions remain unclear. Therefore, we recombinantly produced desiccation-induced LEA4 protein member, RsLEAP30-His6, from Ramonda serbica and investigated its structural behaviour under simulated dehydration conditions. This is the first report on the production and purification of a recombinant LEA protein from the resurrection plant R. serbica. By immobilised metal affinity and size-exclusion chromatography, we successfully obtained RsLEAP30-His6 with a purity of over 95%, thus providing a robust and scalable method that can also be used for the production of other LEA proteins. Structural characterisation by circular dichroism spectroscopy in combina

SUBMITTER: Pantelic A 

PROVIDER: S-EPMC12501365 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature