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Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum.

Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum. Research Abstract Details 

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  • Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum. Abstract Text:

    sergio barranco-medinaSergio Barranco-Medina,tino krellTino Krell,iris finkemeierIris Finkemeier,francisca sevillaFrancisca Sevilla, ,karl-josef dietzKarl-Josef Dietz,

    The pea peroxiredoxin homologue PsPrxII F of the Arabidopsis thaliana mitochondrial AtPrxII F was isolated as cDNA and genomic DNA, and characterized in respect to its biochemical and molecular properties. The deduced amino acid sequence contains an N-terminal targeting address for mitochondrial import. Mitochondrial location of PsPrxII F was confirmed by immunocytochemistry. The mature enzyme, without the transit peptide, has a molecular mass of 18.75 kDa, and, at positions 59 and 84, carries the two catalytic cysteinyl residues which are characteristic for this particular Prx subgroup. Activity of site-directed mutagenized C84S-variant lacking the so-called resolving Cys dropped to about 12% of WT Prx while C59S lost its peroxidatic activity completely. Likewise, WT PsPrxII F and C84S-variant but not C59S protected plasmid DNA against strand breakage in a mixed function oxidation assay. WT PrxII F and the variant proteins aggregated to high mass oligomers not yet described for type II Prx. Upon oxidation with hydrogen peroxide PsPrxII F focussed in a series of spots of distinct pI but similar molecular masses in two-dimensional gels indicating different oxidation states of the protein. Using this technique, partial oxidation was also detected in leaf extracts and isolated mitochondria. PsPrxII F mRNA and protein accumulated in cold and heavy metals treated pea plants suggesting a particular function under stress.

    Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum. Publishing Authors By Initials

    s barranco-medinaS Barranco-Medina,t krellT Krell,i finkemeierI Finkemeier,f sevillaF Sevilla,jj JJ ,kj dietzKJ Dietz,

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    Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Plant physiology and biochemistry : PPB / Société

    VOLUME: 45

    Page Numbers: 729-39

    Journal Abbreviation: Plant Physiol. Biochem.

    ISSN: 0981-9428

    DAY: 7

    MONTH: 08

    YEAR: 2007

    Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum. Information

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    LANGUAGE: eng

    NlmUniqueID: 9882449

    Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum. Keywords Mesh Terms:

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    Grant and Affiliation Information for Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum.

    AFFILIATION: Department of Biochemistry and Cellular and Molecular Biology of Plants, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, E-18008 Granada, Spain.

    Country: France

    France Research PublicationFrance Research Publication

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    MEDLINETA: Plant Physiol Biochem

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