Processing in vitro of precursor periplasmic proteins from Escherichia coli.
Precursors of two secreted periplasmic proteins in Escherichia coli, arabinose-binding protein and maltose-binding protein, were synthesized in vitro on membrane-bound polysomes. Addition of Triton X-100 to the system resulted in processing of the precursors to mature forms.
D001089:Arabinose; D001426:Bacterial Proteins / Q000096:biosynthesis*; D002352:Carrier Proteins / Q000096:biosynthesis; D002701:Chloramphenicol / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism; D008320:Maltose; D008715:Methionine / Q000378:metabolism; D010447:Peptide Hydrolases; D011092:Polyethylene Glycols / Q000494:pharmacology; D011132:Polyribosomes / Q000378:metabolism; D011498:Protein Precursors / Q000096:biosynthesis*; D011691:Puromycin / Q000494:pharmacology
D001426:Bacterial Proteins; D002352:Carrier Proteins; D011498:Protein Precursors; D011092:Polyethylene Glycols; D011691:Puromycin; D002701:Chloramphenicol; D008320:Maltose; D008715:Methionine; D001089:Arabinose; D010447:Peptide Hydrolases