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- Publisher
- Wiley
- Copyright
- Copyright © 2002 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 0140-7791
- eISSN
- 1365-3040
- DOI
- 10.1046/j.1365-3040.2002.00858.x
- Publisher site
- See Article on Publisher Site
Abstract
The PR‐10c (previously termed as Bet v 1‐Sc3) protein of birch belongs to the family of intracellular pathogenesis‐related proteins. The high‐performance liquid chromatography electrospray ionization ion trap mass spectrometry (HPLC‐ESI‐MS) analysis of PR‐10c‐His fusion protein, produced in Escherichia coli, revealed three major peaks and masses. Enzymatic digestions and HPLC‐ESI‐MS and matrix assisted laser desorption/ionization – time of flight mass spectrometry (MALDI‐TOF‐MS) analyses of each fraction indicated that PR‐10c‐His protein is post‐translationally modified by carbamylation and S‐glutathiolation. Carbamylation was localized into the N‐terminal end of PR‐10c‐His and does not represent a biologically significant modification. The possible nuclease activity of PR‐10c was analysed with S‐glutathiolated and reduced fractions of PR‐10c‐His fusion protein. Both forms of PR‐10c‐His as well as the dimeric form of the protein possess RNase activity which is capable of digesting different RNA substrates. None of the fractions showed activity against single‐ or double‐stranded DNA. The MALDI‐TOF‐MS analysis of PR‐10c polypeptide extracted from zinc‐exposed birch roots showed that the protein is post‐translationally modified by glutathione (γ‐Glu‐Cys‐Gly) also in vivo. The S‐glutathiolated cysteine residue of PR‐10c is not conserved among Bet v 1 homologous proteins and is also unique in the PR‐10 family. As far as we know this is the first observation of S‐glutathiolation in plants, or any post‐translational modification in the PR‐10 family of proteins.
Journal
Plant Cell & Environment – Wiley
Published: Jun 1, 2002