Open AccessSoluble factors stimulating secretory protein translocation in bacteria and yeast can substitute for each other.
Author(s) -
Irene T. Fecycz,
Günter Blobel
Publication year - 1987
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.84.11.3723
Subject(s) - yeast , chromosomal translocation , saccharomyces cerevisiae , escherichia coli , biochemistry , membrane , biology , microsome , secretion , microbiology and biotechnology , chemistry , gene , in vitro
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.