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Characterization of a strawberry late‐expressed and fruit‐specific peptide methionine sulphoxide reductase
Author(s) -
Lopez Andrés Pedraza,
Portales Rosario Blanco,
LópezRáez Juan Antonio,
MedinaEscobar Nieves,
Blanco Juan Muñoz,
Franco Antonio Rodríguez
Publication year - 2006
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.2005.00580.x
Subject(s) - achene , methionine , complementary dna , biochemistry , biology , fragaria , reductase , peptide sequence , enzyme , microbiology and biotechnology , amino acid , gene , botany
We have cloned and characterized a cDNA clone, called Fapmsr , coding for a putative peptide methionine sulphoxide [Met(O)] reductase (PMSR, EC 1.8.4.6) from strawberry fruits ( Fragaria x ananassa ). This gene is involved in the repair of inactive peptides and proteins caused for the oxidation of methionine residues to Met(O). Expression of the Fapmsr was only detected in the receptacles of red mature fruits and not in young or immature fruits nor in other plant tissues such as flowers, leaves, runners, roots or achenes. Expression of the Fapmsr gene was activated in green immature fruits when achenes were removed from receptacles, and this was prevented by the application of exogenous auxins such as naphthaleneacetic acid. The enzyme produced and purified by cloning the strawberry cDNA in frame with the C‐terminal sequence of the glutathione S‐transferase gene can reduce free Met(O) to methionine as analysed by reverse phase high performance liquid chromatography. We have also set up a PMSR protection assay that demonstrates that this enzyme can protect in vivo against the damage produced by the addition of H 2 O 2 .