High impact information on Jafrac1

• The Thioredoxin Specificity of Drosophila GPx: A Paradigm for a Peroxiredoxin-like Mechanism of many Glutathione Peroxidases [1].
• Like other CysGPxs with thioredoxin peroxidase activity, Drosophila melanogaster (Dm)GPx oxidized by H(2)O(2) contained an intra-molecular disulfide bridge between the active-site cysteine (C45; C(P)) and C91 [1].
• We identified an Anopheles stephensi 2-Cys Prx ortholog of Drosophila melanogaster Prx-4783, which protects fly cells against oxidative stresses [2].
• A putative glutathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity [3].
• In 2D gels the antibody not only recognizes the SSP5111 polypeptide but also a related one (catalogued in the database as SSP6107) that exhibits identical amino-acid sequence over at least 85% of its sequence [4].

Biological context of Jafrac1

• The B. mori TPx (BmTPx) cDNA contains an open reading frame of 585 bp encoding 195 amino acid residues and possesses two cysteine residues that are characteristic of 2-Cys subgroup of peroxiredoxin family [5].
• One of them, Jafrac1, encodes the SSP5111 protein searched, had 194 amino acids and mapped in the region 11E in the X chromosome [4].
• The eclosion and oviposition rhythms of flies from a population of Drosophila melanogaster maintained under constant conditions of the laboratory were assayed under constant light (LL), constant darkness (DD), and light/dark (LD) cycles of 10:10h (T20), 12:12h (T24), and 14:14h (T28) [6].

Other interactions of Jafrac1

• The deduced amino acid sequence of the GoPrx cDNA showed 69% identity to Drosophila melanogaster DPx-2540, 50% to D. melanogaster DPx-6005, and 47% to Glossina morsitans morsitans Prx [7].

Analytical, diagnostic and therapeutic context of Jafrac1

• 2D gel electrophoresis followed by microsequencing has been used to purify and identify a protein (catalogued in the database as SSP5111) from Drosophila wing imaginal discs of third instar larvae that showed significant differences in their level of expression when compared with other imaginal discs of the same age [4].
• Molecular cloning and characterization of a peroxiredoxin gene from the mole cricket, Gryllotalpa orientalis [7].
• Sequence analysis of an evolutionarily conserved stress-responsive protein, Drosophila Peroxiredoxin I (dPrx I), found the transcript to have two alternative 5'UTRs that lead to an identical coding sequence: namely Ia and Ib [8].

References