Proteins of ribosome-bearing and free-membrane domains in Bacillus subtilis.
In lysates of Bacillus subtilis a free-membrane fraction without ribosomes can be separated from the denser membrane-ribosome complexes. As determined by one-dimensional sodium dodecyl sulfate gel electrophoresis, these two fractions differ markedly in protein composition; at least six major bands (molecular weights, 130,000, 92,000, 68,000, 64,000, 45,000, and 31,000) are essentially unique to the complexed-membrane fraction (CM proteins), and two are unique to the free-membrane fraction. After growth was slowed, the proportion of the free-membrane fraction increased, but the composition of this fraction was the same, whereas after puromycin treatment, which abruptly increased the proportion of the free-membrane fraction, this fraction contained CM proteins. Thus, it appears that the two fractions recovered from growing cells represent topographically and functionally distinct domains. In addition, the effect of growth rate suggests that formation of the complexed domain is regulated at least roughly in parallel with the formation of ribosomes. The separation of these membrane fractions should facilitate the study of protein secretion, membrane topography, and morphogenesis in bacteria.
D001412:Bacillus subtilis / Q000032:analysis* / Q000254:growth & development / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000032:analysis*; D002458:Cell Fractionation; D002462:Cell Membrane / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis*; D008970:Molecular Weight; D011691:Puromycin / Q000494:pharmacology; D012270:Ribosomes / Q000032:analysis*; D013010:Sonication
D001426:Bacterial Proteins; D008565:Membrane Proteins; D011691:Puromycin