Molecular characterization of the Drosophila Mo25 gene, which is conserved among Drosophila, mouse, and yeast

DNA Cell Biol. 1996 Jun;15(6):505-9. doi: 10.1089/dna.1996.15.505.


To study the general physiological role of the Mo25 gene, which has been cloned from mouse cleavage-stage embryos, we isolated a Drosophila equivalent, dMo25, cDNA from an embryo cDNA library. The 2,222 nucleotides contained a single open reading frame encoding a polypeptide of 339 amino acid residues with a calculated molecular mass of 39,278 daltons. The deduced amino acid sequence of the dMo25 cDNA had 69.3% identity with mouse Mo25. A homology search revealed that these were similar to a protein encoded in an open reading frame near the calcineurin B subunit gene on chromosome XI in Saccharomyces cerevisiae. In particular, the carboxy-terminal region was highly conserved in Drosophila, mouse, and yeast. The dMo25 gene was mapped to the left arm of the third chromosome at 73AB, and 2.3- and 1.8-kb mRNA bands were detected during development and in adult Drosophila. Conservation of the gene structure and the wide expression profile indicated that the function of the gene is likely to be fundamental in many cell types as well as during development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Chromosome Mapping
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Drosophila / embryology
  • Drosophila / genetics*
  • Drosophila Proteins*
  • Embryo, Nonmammalian
  • Gene Expression Regulation, Developmental
  • Genes / genetics*
  • Mice
  • Molecular Sequence Data
  • Open Reading Frames / genetics
  • Proteins / genetics*
  • RNA, Messenger / analysis
  • Saccharomyces cerevisiae / genetics*
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid


  • DNA, Complementary
  • Drosophila Proteins
  • Mo25 protein, Drosophila
  • Proteins
  • RNA, Messenger

Associated data

  • GENBANK/AB000402