Secretory protein synthesis in Chironomus salivary gland cells is not coupled with protein translocation across endoplasmic reticulum membranes
- 6 November 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 257 (2) , 251-253
- https://doi.org/10.1016/0014-5793(89)81545-5
Abstract
Fragments of rough endoplasmic reticulum containing polysomes bound to the membranes only at the 5' end were visualized in electron microscopic spreads from Chironomus thummi salivary gland cells. The length of the nascent protein molecules in the polysemes increased from the 5' to the 3' (free) polysome end. The data obtained disagree with the generally accepted model according to which synthesis of secretory proteins is concomitant with the protein transport across the endoplasmic membraneKeywords
This publication has 14 references indexed in Scilit:
- How proteins move across the endoplasmic reticulum membraneHepatology, 1987
- Mechanism of Protein Translocation Across the Endoplasmic Reticulum MembraneAnnual Review of Cell Biology, 1986
- Large sized nascent protein as dominating component during protein synthesis in Chironomus salivary glandsChromosoma, 1980
- Direct association of Balbiani ring 75S RNA with membranes of the endoplasmic reticulumNature, 1977
- Large-sized polysomes in Chironomus tentans salivary glands and their relation to Balbiani ring 75S RNA.The Journal of cell biology, 1977
- Intracellular Aspects of the Process of Protein SynthesisScience, 1975
- MORPHOLOGICAL STUDIES OF TRANSCRIPTIONActa Endocrinologica, 1972
- Ribosome-Membrane Interaction in Eukaryotic CellsPublished by Springer Nature ,1971