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Tropomyosin is an interaction partner of the Drosophila coiled coil protein yuri gagarin
Authors:Texada Michael J  Simonette Rebecca A  Deery William J  Beckingham Kathleen M
Institution:aDepartment of Biochemistry and Cell Biology, Rice University, MS-140, 6100 Main Street, Houston TX 77005, USA
Abstract:The Drosophila gene yuri gagarin is a complex locus encoding three protein isoform classes that are ubiquitously expressed in the organism. Mutations to the gene affect processes as diverse as gravitactic behavior and spermatogenesis. The larger Yuri isoforms contain extensive coiled-coil regions. Our previous studies indicate that one of the large isoform classes (Yuri-65) is required for formation of specialized F-actin-containing structures generated during spermatogenesis, including the so-called actin “cones” that mediate spermatid individualization. We used the tandem affinity purification of a tagged version of Yuri-65 (the TAP-tagging technique) to identify proteins associated with Yuri-65 in the intact organism. Tropomyosin, primarily as the 284-residue isoform derived from the ubiquitously expressed Tropomyosin 1 gene was thus identified as a major Yuri interaction partner. Co-immunoprecipitation experiments confirmed this interaction. We have established that the stable F-actin cones of spermatogenesis contain Tropomyosin 1 (Tm1) and that in mutant yuriF64, failure of F-actin cone formation is associated with failure of Tm1 to accumulate at the cone initiation sites. In investigating possible interactions of Tm1 and Yuri in other tissues, we discovered that Tm1 and Yuri frequently colocalize with the endoplasmic reticulum. Tropomyosin has been implicated in actin-mediated membrane trafficking activity in other systems. Our findings suggest that Yuri–Tm1 complexes participate in related functions.
Keywords:Abbreviations: GFP  Green Fluorescent Protein  SDS-PAGE  sodium dodecyl sulfate polyacrylamide gel electrophoresis  MW  molecular weight  HRP  horse radish peroxidase  DTT  dithiothreitol  EDTA  ethylene diamine tetraacetic acid  EGTA  ethylene glycol tetraacetic acid
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