Back to Search
Start Over
The clot gene of Drosophila melanogaster encodes a conserved member of the thioredoxin-like protein superfamily
- Source :
- Europe PubMed Central, Scopus-Elsevier
- Publication Year :
- 2002
-
Abstract
- The conversion of pyruvoyl-H4-pterin to pyrimidodiazepine (PDA), which is an essential step in the biosynthesis of the red components of Drosophila eye pigments known as drosopterins, requires the products of the genes sepia and clot. While the product of sepia has been shown to correspond to the enzyme PDA-synthase, the role of clot remains unknown, although the clot 1 allele was one of the first eye-color mutants to be isolated in Drosophila melanogaster, and much genetic and biochemical data has become available since. Here we report the cloning of the clot gene, describe its molecular organization and characterize the sequence alterations associated with the alleles cl 1 and cl 2 . The coding properties of the gene show that it encodes a protein related to the Glutaredoxin class of the Thioredoxin-like enzyme superfamily, conserved members of which are found in human, mouse and plants. We suggest that the Clot protein is an essential component of a glutathione redox system required for the final step in the biosynthetic pathway for drosopterins.
- Subjects :
- Mutant
Molecular Sequence Data
Genes, Insect
Protein Structure, Secondary
Mice
Thioredoxins
Glutaredoxin
Genetics
Animals
Drosophila Proteins
Humans
Amino Acid Sequence
Allele
Sepia
Cloning, Molecular
Molecular Biology
Gene
Conserved Sequence
Glutaredoxins
Cloning
biology
Base Sequence
Sequence Homology, Amino Acid
Pteridines
Genetic Complementation Test
Gene Expression Regulation, Developmental
Proteins
General Medicine
DNA
Protein superfamily
biology.organism_classification
Glutathione
Cell biology
Drosophila melanogaster
Oxidoreductases
Oxidation-Reduction
Subjects
Details
- ISSN :
- 16174615
- Volume :
- 268
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- Molecular genetics and genomics : MGG
- Accession number :
- edsair.doi.dedup.....8e863bfd33f330535282bdf0e9638124