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Molecular characterization of a novel patched‐related protein in Apis mellifera and Drosophila melanogaster
Author(s) -
Pastenes Luis,
Ibáñez Freddy,
Bolatto Carmen,
Pavéz Leonardo,
Cambiazo Verónica
Publication year - 2008
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20245
Subject(s) - drosophila melanogaster , biology , transmembrane domain , transmembrane protein , gene , melanogaster , membrane protein , microbiology and biotechnology , protein domain , genetics , membrane , receptor
The molecular identification and characterization of the patched‐related ( ptr ) gene and protein in Apis mellifera and Drosophila melanogaster are reported. Ptr proteins are closely related in predicted topology and domain organization to the protein encoded by the Drosophila segment polarity gene patched . Ptrs have 12 potential transmembrane domains arranged in two sets of 1+5 membrane‐spanning segments containing a conserved sterol‐sensing domain (SSD) and functional GxxxD and PPXY motifs. Phylogenetic analysis showed that Ptrs belong to a previously uncharacterized class of insect proteins that share a high level of sequence identity. Analysis using quantitative real‐time polymerase chain reaction (qPCR) indicates that ptr gene is preferentially expressed during embryo stages of A. mellifera development; interestingly, this pattern of temporal expression was also observed for the D. melanogaster homologue, suggesting that these proteins might be involved in embryo morphogenesis. To understand Ptr function at the molecular level, we investigated the subcellular distribution of Dm Ptr. We have shown by biochemical analysis that Dm Ptr protein is tightly associated with membranes. Consistently, Ptr immunoreactivity appears to be localized at the sites of membrane furrow formation during cellularization of D. melanogaster embryos. These studies indicated that Ptrs belong to a previously uncharacterized class of insect transmembrane proteins that share a high level of sequence identity. Our analysis of ptr gene expression and protein localization suggest that Ptr might fulfil a developmental role by participating in processes that require growth and stabilization of plasma membrane. Arch. Insect Biochem. Physiol. 68:156–170, 2008. © 2008 Wiley‐Liss, Inc.