Signal peptides and signal peptidase in Drosophila melanogaster
| Autor: | Thomas G. Warren, Mark D. Brennan, Anthony P. Mahowald |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Signal peptide
Macromolecular Substances Lipoproteins Biology Vitellogenins Reticulocyte Species Specificity Microsomes Endopeptidases medicine Animals Amino Acid Sequence Protein Precursors Peptide sequence Gel electrophoresis Signal peptidase Molecular mass Ovary Serine Endopeptidases RNA Membrane Proteins Cell Biology Articles biology.organism_classification Peptide Fragments Molecular Weight medicine.anatomical_structure Drosophila melanogaster Biochemistry Female |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 0021-9525 |
| Popis: | Translation of poly(A)-containing RNA from the female fat body of Drosophila melanogaster in a rabbit reticulocyte cell-free system results in the synthesis of previtellogenin polypeptides (PVs) having higher apparent molecular weights (46,000 and 45,000) than the forms seen after an in vivo pulse labeling. However, when this RNA is translated in the presence of EDTA-stripped microsomal membranes from the dog pancreas, vitellogenin precursors are produced that, upon SDS-polyacrylamide gel electrophoresis, comigrate with the in vivo forms (apparent molecular weights, 45,000 and 44,000). These processed forms are sequestered within the microsomal lumen, as evidenced by their insensitivity to trypsin digestion. Neither processing nor sequestration occur posttranslationally. In addition, a microsomal membrane fraction derived from Drosophila embryos is able to cotranslationally process the PVs as well as a murine pre-light chain IgG. These observations support a signal-mediated mode of secretion in Drosophila, and suggest that signal sequence recognition and signal peptidase activities are conserved even between mammalian and insect systems. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|