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. 1985 Jun;82(12):4031–4035. doi: 10.1073/pnas.82.12.4031

Secretory S complex of Bacillus subtilis forms a large, organized structure when released from ribosomes.

M P Caulfield, D Furlong, P C Tai, B D Davis
PMCID: PMC397928  PMID: 3923486

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.

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