Soluble factors stimulating secretory protein translocation in bacteria and yeast can substitute for each other.
mRNA for prepro-alpha-factor (pp alpha), a yeast secretory glycoprotein, was translated in a wheat germ cell-free system that was posttranslationally supplemented either with inverted vesicles from the plasma membrane of Escherichia coli (INV) or with microsomes from Saccharomyces cerevisiae. A postribosomal supernatant (PRS) from E. coli was found to stimulate translocation of pp alpha across the INV membrane. A yeast PRS could substitute for its E. coli counterpart. Likewise, an E. coli PRS could substitute for a yeast PRS and stimulate translocation of pp alpha across yeast microsomal membranes.
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D001426:Bacterial Proteins / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D005656:Fungal Proteins / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D005800:Genes, Fungal; D007425:Intracellular Membranes / Q000378:metabolism; D008861:Microsomes / Q000378:metabolism; D010944:Plants / Q000378:metabolism; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000235:genetics*; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D014158:Transcription, Genetic; D014908:Triticum / Q000378:metabolism
D001426:Bacterial Proteins; D005656:Fungal Proteins; C048632:MF(ALPHA)1 protein, S cerevisiae; D011498:Protein Precursors; D029701:Saccharomyces cerevisiae Proteins