Secretory S complex of Bacillus subtilis forms a large, organized structure when released from ribosomes.
- 1 June 1985
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 82 (12) , 4031-4035
- https://doi.org/10.1073/pnas.82.12.4031
Abstract
The S complex of Bacillus subtilis, a set of four proteins that appears to be involved in protein secretion, is shown to be attached to 70S ribosomes: antibody to its 64-kDa component can aggregate these ribosomes, and the complex can be chemically crosslinked to ribosomal proteins. Low Mg2+ or prolonged high-speed centrifugation in a sucrose gradient releases the S complex from the ribosomes, and it is recovered as an aggregate with an S value of 76. Electron microscopy shows that these aggregates have a regular structure, somewhat resembling clathrin cages, with a diameter of about 45 nm. If these aggregates are physiological, their function would differ significantly from that of the signal recognition particle of eukaryotes.This publication has 23 references indexed in Scilit:
- In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli.Proceedings of the National Academy of Sciences, 1984
- The 64-kilodalton membrane protein of Bacillus subtilis is also present as a multiprotein complex on membrane-free ribosomes.Proceedings of the National Academy of Sciences, 1984
- A 64-kilodalton membrane protein of Bacillus subtilis covered by secreting ribosomes.Proceedings of the National Academy of Sciences, 1983
- Polymerization of clathrin protomers into basket structuresBiochemistry, 1981
- Coated vesicles transport newly synthesized membrane glycoproteins from endoplasmic reticulum to plasma membrane in two successive stages.Proceedings of the National Academy of Sciences, 1980
- [12] Practical aspects of immune electron microscopyPublished by Elsevier ,1979
- Identification of fifteen neighboring protein pairs in the Escherichia coli 50 S ribosomal subunit crosslinked with 2-iminothiolaneJournal of Molecular Biology, 1979
- Coated vesicles from pig brain: Purification and biochemical characterizationJournal of Molecular Biology, 1975
- Pressure-Induced Dissociation of Sedimenting Ribosomes: Effect on Sedimentation PatternsProceedings of the National Academy of Sciences, 1971
- Electron microscopy of an antibody-hapten complexJournal of Molecular Biology, 1967