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Desiccation of the resurrection plant Craterostigma plantagineum induces dynamic changes in protein phosphorylation
Author(s) -
RÖHRIG HORST,
SCHMIDT JÜRGEN,
COLBY THOMAS,
BRÄUTIGAM ANNE,
HUFNAGEL PETER,
BARTELS DOROTHEA
Publication year - 2006
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.2006.01537.x
Subject(s) - phosphorylation , desiccation tolerance , dehydration , protein phosphorylation , desiccation , abscisic acid , biology , biochemistry , microbiology and biotechnology , chemistry , botany , protein kinase a , gene
ABSTRACT Reversible phosphorylation of proteins is an important mechanism by which organisms regulate their reactions to external stimuli. To investigate the involvement of phosphorylation during acquisition of desiccation tolerance, we have analysed dehydration‐induced protein phosphorylation in the desiccation tolerant resurrection plant Craterostigma plantagineum . Several dehydration‐induced proteins were shown to be transiently phosphorylated during a dehydration and rehydration (RH) cycle. Two abundantly expressed phosphoproteins are the dehydration‐ and abscisic acid (ABA)‐responsive protein CDeT11‐24 and the group 2 late embryogenesis abundant (LEA) protein CDeT6‐19. Although both proteins accumulate in leaves and roots with similar kinetics in response to dehydration, their phosphorylation patterns differ. Several phosphorylation sites were identified on the CDeT11‐24 protein using liquid chromatography‐tandem mass spectrometry (LC‐MS/MS). The coincidence of phosphorylation sites with predicted coiled‐coil regions leads to the hypothesis that CDeT11‐24 phosphorylations influence the stability of coiled‐coil interactions with itself and possibly other proteins.