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Identifying Protein-protein Interaction in Drosophila Adult Heads by Tandem Affinity Purification (TAP)
Published on: December 6, 2013
Interspecific comparisons reveal conserved features of the Drosophila Toll protein
M Yamagata1, J P Merlie, J R Sanes
1Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, MO 63110.
Abstract:
The Toll gene of Drosophila melanogaster produces a transmembrane cell adhesion protein that is required to establish the dorso-ventral axis of the embryo. The Toll protein's extracellular domain contains Leu-rich repeats (LRR), implicated in intermolecular interactions, and its large intracellular domain transduces a signal that eventually reaches the nucleus. Here, we report amino-acid (aa) sequences encoded by the Toll genes of D. pseudoobscura and D. virilis, and two distinct Toll-like genes of the grasshopper, Schistocerca americana. Interspecific comparisons show a Toll-specific subfamily of LRR, and a strikingly high degree of conservation in the cytoplasmic domain. Interestingly, many aa residues conserved among the insect Toll-like cytoplasmic domains are also conserved in mammalian and avian type-I interleukin-1 receptors and the hypothetical product of a transcript, MyD88, found in murine myeloid cells. Thus, we identify a set of conserved aa in the cytoplasmic domain which might be used in a signal-transduction pathway shared by invertebrates and vertebrates.
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