Post-translational modification of barley 14-3-3A is isoform-specific and involves removal of the hypervariable C-terminus

Christa Testerink, Mieke J. Van Zeijl, Katrine Drumm, Michael G. Palmgren, David B. Collinge, Jan W. Kijne, Mei Wang*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

19 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)535-542
Number of pages8
JournalPlant Molecular Biology
Volume50
Issue number3
DOIs
Publication statusPublished - 1 Oct 2002
Externally publishedYes

Keywords

  • 14-3-3 Protein
  • H+-ATPase
  • Hordeum distichum
  • Post-translational modification
  • Proteolytic cleavage

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