Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum
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 imp...
| Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 45(2007), 10-11 vom: 15. Okt., Seite 729-39 |
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| Weitere Verfasser: | , , , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2007
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| Zugriff auf das übergeordnete Werk: | Plant physiology and biochemistry : PPB |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Metals, Heavy Mitochondrial Proteins Plant Proteins RNA, Messenger Hydrogen Peroxide BBX060AN9V Peroxiredoxins EC 1.11.1.15 |
| Zusammenfassung: | 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 |
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| Beschreibung: | Date Completed 28.02.2008 Date Revised 09.01.2024 published: Print-Electronic GENBANK: AM411615 ErratumIn: Plant Physiol Biochem. 2021 Apr;161:259. doi: 10.1016/j.plaphy.2021.02.004. - PMID 33602556 Citation Status MEDLINE |
| ISSN: | 1873-2690 |