TAILIEUCHUNG - Báo cáo khoa học: Plasmoredoxin, a novel redox-active protein unique for malarial parasites

Thioredoxins are a group of small redox-active proteins involved in cellular redox regulatory processes as well as antioxidant defense. Thioredoxin, glutaredoxin, and try-paredoxin are members of the thioredoxin superfamily and share structural and functional characteristics. In the mal-arial parasite, Plasmodium falciparum, a functional thio-redoxin and glutathione system have been demonstrated and are considered to be attractive targets for antimalarial drug development. | Eur. J. Biochem. 270 1057-1064 2003 FEBS 2003 doi PRIORITY PAPER Plasmoredoxin a novel redox-active protein unique for malarial parasites Katja Becker1 Stefan M. Kanzok2 Rimma lozef1 Marina Fischer1 R. Heiner Schirmer2 and Stefan Rahlfs1 1 Interdisciplinary Research Center Justus-Liebig-University D-35392 Giefien Germany 2Biochemistry Center Ruprecht-Karls-University D-69120 Heidelberg Germany Thioredoxins are a group of small redox-active proteins involved in cellular redox regulatory processes as well as antioxidant defense. Thioredoxin glutaredoxin and try-paredoxin are members of the thioredoxin superfamily and share structural and functional characteristics. In the malarial parasite Plasmodium falciparum a functional thioredoxin and glutathione system have been demonstrated and are considered to be attractive targets for antimalarial drug development. Here we describe the identification and characterization of a novel 22 kDa redox-active protein in P. falciparum. As demonstrated by in silico sequence analyses the protein named plasmoredoxin Plrx is highly conserved but found exclusively in malarial parasites. It is a member of the thioredoxin superfamily but clusters separately from other members in a phylogenetic tree. We amplified the gene from a gametocyte cDNA library and overexpressed it in E. coli. The purified gene product can be reduced by glutathione but much faster by dithiols like thioredoxin glutaredoxin try-panothione and tryparedoxin. Reduced Plrx is active in an insulin-reduction assay and reduces glutathione disulfide with a rate constant of 640 M-1-s-1 at pH and 25 C glutathione-dependent reduction of H2O2 and hydroxyethyl disulfide by Plrx is negligible. Furthermore plasmoredoxin provides electrons for ribonucleotide reductase the enzyme catalyzing the first step of DNA synthesis. As demonstrated by Western blotting the protein is present in blood-stage forms of malarial parasites. Based on these results .

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