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Gene Review

ari-2  -  ariadne 2

Drosophila melanogaster

Synonyms: AAF46823.1, Ari-2, CG5709, Dmel\CG5709, Protein ariadne-2, ...
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High impact information on ari-2

  • Thus, tafazzin mutations in Drosophila generated a Barth-related phenotype, with the triad of abnormal cardiolipin, pathologic mitochondria, and motor weakness, suggesting causal links between these findings [1].
  • However, substitution of the zinc-binding cysteine residue by serine, along with an altered coordinating histidine residue, assembles a constellation of residues that resembles a modified catalytic triad [2].
  • The catalytic triad in Drosophila alcohol dehydrogenase: pH, temperature and molecular modelling studies [3].
  • The mutations introduce amino acid substitutions that are larger than the corresponding wild-type residues and are located within the active site of the enzyme, close to the catalytic triad [4].
  • The triad of a presacral tumour, sacral agenesis and anorectal malformation constitutes the Currarino syndrome which is caused by dorsal-ventral patterning defects during embryonic development [5].

Biological context of ari-2

  • Three characteristic features, (i) a catalytic triad of serine proteases, (ii) two PDZ domains and (iii) a putative signal peptide, classify the endobacterial protein as a member of the periplasmic HtrA family of proteases known to express chaperone and regulator activity of apoptosis [6].

Anatomical context of ari-2

  • LIS1 is hypothesized to regulate nuclear movement in migrating neurons through interactions with the cytoskeleton, while the alpha-subunits, whose structure is known, contain a trypsin-like triad within the framework of a unique tertiary fold [7].

Associations of ari-2 with chemical compounds

  • All of the mature proteases contained the histidine, aspartic acid and serine amino acids of the catalytic triad characteristic of serine proteases [8].
  • The 45-kDa protein contained a trypsin-like serine proteinase domain at the C-terminus, except for the substitution of Ser of the active site triad to Gly and had a disulfide-knotted domain at the N-terminus [9].
  • The three residues (Ser, Glu and His) that putatively form the catalytic triad and the six Cys that form intra-subunit disulfide bonds were completely conserved when compared to the other seven AChEs from a broad range of animal species reported to date [10].
  • Furthermore, the critical DDE catalytic triad of RAG1 is shared with the Transib transposase as part of conserved motifs [11].

Other interactions of ari-2

  • Sequencing of one of the putative esterase genes in the Drosophila cluster, alpha E1, shows that it would encode features characteristic of an active carboxyl/cholinesterase, including the so-called catalytic triad, the nucleophilic elbow and oxyanion hole [12].
  • This Tenebrio masquerade-like serine proteinase homologue (Tm-mas) contains a trypsin-like serine proteinase domain in the C-terminal region, except for the substitution of Ser to Gly at the active site triad, and a disulfide-knotted domain at the amino-terminal region [13].

Analytical, diagnostic and therapeutic context of ari-2


  1. A Drosophila model of Barth syndrome. Xu, Y., Condell, M., Plesken, H., Edelman-Novemsky, I., Ma, J., Ren, M., Schlame, M. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Crystal structure of the Drosophila peptidoglycan recognition protein (PGRP)-SA at 1.56 A resolution. Reiser, J.B., Teyton, L., Wilson, I.A. J. Mol. Biol. (2004) [Pubmed]
  3. The catalytic triad in Drosophila alcohol dehydrogenase: pH, temperature and molecular modelling studies. Winberg, J.O., Brendskag, M.K., Sylte, I., Lindstad, R.I., McKinley-McKee, J.S. J. Mol. Biol. (1999) [Pubmed]
  4. Identification and characterization of mutations in housefly (Musca domestica) acetylcholinesterase involved in insecticide resistance. Walsh, S.B., Dolden, T.A., Moores, G.D., Kristensen, M., Lewis, T., Devonshire, A.L., Williamson, M.S. Biochem. J. (2001) [Pubmed]
  5. Spectrum of mutations and genotype-phenotype analysis in Currarino syndrome. Köchling, J., Karbasiyan, M., Reis, A. Eur. J. Hum. Genet. (2001) [Pubmed]
  6. Wolbachia endosymbionts of Onchocerca volvulus express a putative periplasmic HtrA-type serine protease. Jolodar, A., Fischer, P., Büttner, D.W., Brattig, N.W. Microbes Infect. (2004) [Pubmed]
  7. Homologs of the alpha- and beta-subunits of mammalian brain platelet-activating factor acetylhydrolase Ib in the Drosophila melanogaster genome. Sheffield, P.J., Garrard, S., Caspi, M., Aoki, J., Arai, H., Derewenda, U., Inoue, K., Suter, B., Reiner, O., Derewenda, Z.S. Proteins (2000) [Pubmed]
  8. Cloning of a family of serine protease genes from the cat flea Ctenocephalides felis. Gaines, P.J., Sampson, C.M., Rushlow, K.E., Stiegler, G.L. Insect Mol. Biol. (1999) [Pubmed]
  9. A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae. Kwon, T.H., Kim, M.S., Choi, H.W., Joo, C.H., Cho, M.Y., Lee, B.L. Eur. J. Biochem. (2000) [Pubmed]
  10. Cloning and sequencing of a cDNA encoding acetylcholinesterase in Colorado potato beetle, Leptinotarsa decemlineata (Say). Zhu, K.Y., Clark, J.M. Insect Biochem. Mol. Biol. (1995) [Pubmed]
  11. RAG1 core and V(D)J recombination signal sequences were derived from Transib transposons. Kapitonov, V.V., Jurka, J. PLoS Biol. (2005) [Pubmed]
  12. Molecular cloning of an alpha-esterase gene cluster on chromosome 3r of Drosophila melanogaster. Russell, R.J., Robin, G.C., Kostakos, P., Newcomb, R.D., Boyce, T.M., Medveczky, K.M., Oakeshott, J.G. Insect Biochem. Mol. Biol. (1996) [Pubmed]
  13. A zymogen form of masquerade-like serine proteinase homologue is cleaved during pro-phenoloxidase activation by Ca2+ in coleopteran and Tenebrio molitor larvae. Lee, K.Y., Zhang, R., Kim, M.S., Park, J.W., Park, H.Y., Kawabata, S., Lee, B.L. Eur. J. Biochem. (2002) [Pubmed]
  14. Mutational analysis of the Drosophila snake protease: an essential role for domains within the proenzyme polypeptide chain. Smith, C., Giordano, H., DeLotto, R. Genetics (1994) [Pubmed]
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