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myo ‐Inositol oxygenase identified in Drosophila melanogaster
Author(s) -
Jones Melissa Kaye,
Eldon Elizabeth D.,
Klig Lisa S.
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.759.13
Subject(s) - drosophila melanogaster , melanogaster , biology , catabolism , inositol , biochemistry , model organism , schneider 2 cells , microbiology and biotechnology , gene , rna interference , enzyme , receptor , rna
myo ‐Inositol oxygenase (MIOX) catalyzes the first committed step in eukaryotic inositol catabolism. In human diabetics, inositol homeostasis is often disturbed through mechanisms that are largely unknown. MIOX is expressed in the kidneys and in extra‐renal tissues where diabetic complications occur. MIOX has not been studied in the model organism Drosophila melanogaster . Establishing that a gene for MIOX exists in D. melanogaster allows for studies of this organism to have cross‐species relevance to humans. The protein encoded by the D. melanogaster CG6910 gene has 54.6% identity to the Mus musculus MIOX protein. CG6910 encodes a protein containing the cognate hairpin loop structure, iron‐binding aspartic acid residue, and PKC binding sites found in mouse and human MIOX. Most of the PKA binding sites are also conserved and novel sites have been found. Flies with CG6910 RNAi ubiquitously activated by an Act5C‐GAL4 driver, similar to carbon/energy starved flies, did not survive more than five days with inositol as the sole carbon/energy source. Western blot analyses reveal decreased MIOX expression in RNAi flies with the Act5C‐GAL4 driver. Other preliminary experiments include a biochemical assay demonstrating MIOX activity in D. melanogaster . These studies indicate that CG6910 encodes MIOX in D. melanogaster and may contribute to understanding the role of inositol catabolism in development and diabetes.