Protein translocation across the yeast microsomal membrane is stimulated by a soluble factor.
We have found that a soluble activity present in the postribosomal supernatant fraction of Saccharomyces cerevisiae stimulates posttranslational translocation of yeast prepro-alpha-factor across yeast microsomal membranes. Stimulation of translocation is not due to a nonspecific affect on ATP levels. The activity is likely to be due to protein(s) as it is destroyed by N-ethylmaleimide, protease, or heat treatment but not by incubation with RNase. Its apparent sedimentation coefficient is approximately 9.6 S.
D001693:Biological Transport, Active; D003593:Cytoplasm / Q000502:physiology; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005656:Fungal Proteins / Q000502:physiology; D000072235:Mating Factor; D008861:Microsomes / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012261:Ribonucleoproteins / Q000502:physiology; D012441:Saccharomyces cerevisiae; D018271:Signal Recognition Particle; D012995:Solubility
D005656:Fungal Proteins; D010455:Peptides; D011498:Protein Precursors; D012261:Ribonucleoproteins; D018271:Signal Recognition Particle; D000072235:Mating Factor