tailieunhanh - Báo cáo Y học: Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana

Understanding peroxidase function in plants is complicated by the lackof substrate specificity, the highnumber of genes, their diversity in structure and our limited knowledge of peroxidase gene transcription and translation. In the present study we sequenced expressed sequence tags (ESTs) enco-ding novel heme-containing class III peroxidases from Arabidopsis thalianaand annotated 73 full-length genes identified in the genome. | Eur. J. Biochem. 269 6063-6081 2002 FEBS 2002 doi Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana Karen G. Welinder1 2 Annemarie F. Justesen1 Inger V. H. Kj rsgard1 Rikke B. Jensen1 Seren K. Rasmussen3 Hans M. Jespersen1 and Laurent Duroux2 1Department of Protein Chemistry University of Copenhagen Denmark department of Biotechnology Aaĩborg University Denmark 3Plant Genetics Ris0 National Laboratory Denmark Understanding peroxidase function in plants is complicated by the lack of substrate specificity the high number of genes their diversity in structure and our limited knowledge of peroxidase gene transcription and translation. In the present study we sequenced expressed sequence tags ESTs encoding novel heme-containing class III peroxidases from Arabidopsis thaliana and annotated 73 full-length genes identified in the genome. In total transcripts of 58 of these genes have now been observed. The expression of individual peroxidase genes was assessed in organ-specific EST libraries and compared to the expression of 33 peroxidase genes which we analyzed in whole plants 3 6 15 35 and 59 days after sowing. Expression was assessed in root rosette leaf stem cauline leaf flower bud and cell culture tissues using the gene-specific and highly sensitive reverse transcriptase-polymerase chain reaction RT-PCR .We predicted that 71 genes could yield stable proteins folded similarly to horseradish peroxidase HRP . The putative mature peroxidases derived from these genes showed 28-94 amino acid sequence identity and were all targeted to the endoplasmic reticulum by N-terminal signal peptides. In 20 peroxidases these signal peptides were followed by various N-terminal extensions of unknown function which are not present in HRP. Ten peroxidases showed a C-terminal extension indicating vacuolar targeting. We found that the majority of peroxidase genes were expressed in root. In total class III peroxidases .

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