INVESTIGADORES
ARAN Martin
congresos y reuniones científicas
Título:
Autophosphorylation of Rapeseed 2-Cys Peroxiredoxin
Autor/es:
ARAN, M.; CAPORALETTI, D.; SENN, A.M.; TELLEZ DE IÑON, M.T.; GIROTTI, M.R.; LLERA, A.S.; WOLOSIUK, R.A.
Lugar:
Mar del Plata, Argentina.
Reunión:
Congreso; XLIII SAIB ANNUAL MEETING; 2007
Institución organizadora:
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Resumen:
2-Cys peroxiredoxins (2-Cys Prx) are
widely distributed thiolcontaining peroxidases that have been implicated in
various cellular processes. We have used functional and structural approaches
to demonstrate that rapeseed 2-Cys Prx is a direct target for nucleotides. The
concerted action of a nucleoside triphosphate and Mg impairs reversibly the
peroxidase activity, being purine derivatives more efficient than pyrimidine
counterparts. In particular, structural and site-directed mutagenesis studies
are consistent with a mechanism where ATP interacts noncovalently with a region
that contains the conserved Cys175. Most importantly, ATP triggers the
autophosphorylation of 2-Cys Prx upon reduction with thiol-bearing compounds or
phosphines followed by oxidation with hydroperoxides, quinones, tetrathionate,
selenate or diamide. Mass spectrometry analysis reveals that 2-Cys Prx
incorporates the phosphoryl moiety into the Cys175 residue yielding the
sulfinic-phosphoryl
[Prx-(Cys175)-SO2PO42-] and the
sulfonic-phosphoryl [Prx-(Cys175)- SO3PO42-] anhydrides.
Hence, the functional coupling betweenATP and 2-Cys Prx brings novel insights
not only to the removal of toxic reactive oxygen species but also to mechanisms
that link the status of cell energy to the oxidation of reactive cysteine
residues.