Post-translational modification of barley 14-3-3A is isoform-specific and involves removal of the hypervariable C-terminus
article
The 14-3-3 protein family is a family of regulatory proteins involved in diverse cellular processes. In a previous study of regulation of individual 14-3-3 isoforms in the germinating barley embryo, we found that a post-translationally modified, 28 kDa form of 14-3-3A was present in specific cell fractions of the germinated embryo. In the present study, we identify the nature of the modification of 14-3-3A, and show that the 28 kDa doublet is the result of cleavage of the C-terminus. The 28 kDa forms of 14-3-3A lack ten or twelve amino acid residues at the non-conserved C-terminus of the protein, respectively. Barley 14-3-3B and 14-3-3C are not modified in a similar way. Like the 30 kDa form, in vitro produced 28 kDa 14-3-3A is still capable of binding AHA2 H+-ATPase in an overlay assay. Our results show a novel isoform-specific post-translational modification of 14-3-3 proteins that is regulated in a tissue-specific and developmental way.
Topics
14-3-3 ProteinH+-ATPaseHordeum distichumPost-translational modificationProteolytic cleavageAmino acidsCellsTissueCellular processesProteins14-3-3 ProteinsAmino Acid SequenceArabidopsis ProteinsBinding SitesBlotting, WesternGerminationHordeumMolecular Sequence DataProtein BindingProtein IsoformsProtein Processing, Post-TranslationalProton-Translocating ATPasesSeedsTyrosine 3-MonooxygenaseEmbryophytaHordeumHordeum vulgare subsp. vulgareStaphylococcus phage 3A
TNO Identifier
72871
ISSN
01674412
Source
Plant Molecular Biology, 50, pp. 535-542.
Pages
535-542
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