TitleA novel basic helix-loop-helix protein is expressed in muscle attachment sites of the Drosophila epidermis.
Publication TypeJournal Article
Year of Publication1994
AuthorsArmand, P, Knapp, AC, Hirsch, AJ, Wieschaus, EF, Cole, MD
JournalMol Cell Biol
Volume14
Issue6
Pagination4145-54
Date Published1994 Jun
KeywordsAmino Acid Sequence, Animals, Base Sequence, Basic Helix-Loop-Helix Transcription Factors, Cloning, Molecular, DNA, Complementary, DNA-Binding Proteins, Drosophila melanogaster, Drosophila Proteins, Embryo, Nonmammalian, Epidermis, Gene Expression, Gene Library, Helix-Loop-Helix Motifs, Mammals, Mice, Molecular Sequence Data, Muscles, Protein Biosynthesis, Sequence Homology, Amino Acid, Transcription Factors, Transcription, Genetic
Abstract

We have found that a novel basic helix-loop-helix (bHLH) protein is expressed almost exclusively in the epidermal attachments sites for the somatic muscles of Drosophila melanogaster. A Drosophila cDNA library was screened with radioactively labeled E12 protein, which can dimerize with many HLH proteins. One clone that emerged from this screen encoded a previously unknown protein of 360 amino acids, named delilah, that contains both basic and HLH domains, similar to a group of cellular transcription factors implicated in cell type determination. Delilah protein formed heterodimers with E12 that bind to the muscle creatine kinase promoter. In situ hybridization with the delilah cDNA localized the expression of the gene to a subset of cells in the epidermis which form a distinct pattern involving both the segmental boundaries and intrasegmental clusters. This pattern was coincident with the known sites of attachment of the somatic muscles to tendon cells in the epidermis. delilah expression persists in snail mutant embryos which lack mesoderm, indicating that expression of the gene was not induced by attachment of the underlying muscles. The similarity of this gene to other bHLH genes suggests that it plays an important role in the differentiation of epidermal cells into muscle attachment sites.

Alternate JournalMol. Cell. Biol.