Freeze-fracture study of the Drosophila photoreceptor membrane: mutations affecting membrane particle density
| Autor: | W L Pak, D C Larrivee, R H Schinz, M V Lo |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Rhodopsin
genetic structures Mutant medicine.disease_cause Cell membrane medicine Animals Freeze Fracturing Photoreceptor Cells Vitamin A Mutation biology Cell Membrane Wild type Articles Intracellular Membranes Cell Biology biology.organism_classification Cell biology Protoplasm Microscopy Electron Drosophila melanogaster Membrane medicine.anatomical_structure biology.protein sense organs |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| DOI: | 10.1083/jcb.93.3.961 |
| Popis: | The photoreceptor membrane of Drosophila melanogaster (wild type, vitamin A-deprived wild type, and the mutants ninaAP228, ninaBP315, and oraJK84) was studied by freeze-fracture electron microscopy. The three mutations caused a decrease in the number of particles on the protoplasmic face of the rhabdomeric membrane. The ninaAP228 mutation affected only the peripheral photoreceptors (R1-6), while the ninaBP315 mutation affected both the peripheral (R1-6) and the central photoreceptors (R7). The oraJK84 mutation, which essentially eliminates R1-6 rhabdomeres, was found to drastically deplete the membrane particles in the vestigial R1-6 rhabdomeres but not in the normal rhabdomeres of R7 photoreceptors, suggesting that the failure of the oraJK84 mutant to form normal R1-6 rhabdomeres may be due to a defect in a major R1-6 photoreceptor-specific protein in the mutant. In all cases in which both the rhabdomeric particle density and rhodopsin content were studied, the mutations or vitamin A deprivation was found to reduce both these quantities, supporting the idea that at least the majority of the rhabdomeric membrane particles are closely associated with rhodopsin. Vitamin A deprivation and the mutations also reduced the number of particles in the plasma membrane as in the rhabdomeric membrane, suggesting that both classes of membrane contain rhodopsin. |
| Databáze: | OpenAIRE |
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