Dbp45A encodes a Drosophila DEAD box protein with similarity to a putative yeast helicase involved in ribosome assembly.
Proteins of the DEAD family of putative ATP-dependent RNA helicases have been implicated in translation initiation, ribosome assembly, and RNA processing in a variety of organisms from Escherichia coli to man. Among these proteins are eIF-4A, an essential component of the cap-binding complex, numerous yeast proteins required for pre-mRNA splicing, and proteins from yeast and E. coli necessary for ribosome assembly. We report the isolation of a new DEAD gene from Drosophila, Dbp45A, which is most abundantly expressed in 6-12 h embryos and adults. The predicted amino acid sequence of the Dbp45A product contains all eight highly conserved DEAD family motifs, and most closely resembles the Saccharomyces cerevisiae DRS1p among known DEAD box proteins. DRS1p has been implicated in ribosomal RNA processing.
Lavoie
C A
CA
Department of Biology, McGill University, Montréal, Québec, Canada.
Harvey
M
M
Lasko
P F
PF
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000196:embryology / Q000235:genetics*; D005784:Gene Amplification; D007301:Insect Hormones / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D012313:RNA / Q000302:isolation & purification; D016601:RNA-Binding Proteins; D016415:Sequence Alignment
C083965:Dbp45A protein, Drosophila; D029721:Drosophila Proteins; D007301:Insect Hormones; D016601:RNA-Binding Proteins; D012313:RNA