Protein export in Escherichia coli.
Hyperproduction of phosphate-binding protein (PhoS) resulted in saturation of export sites, and pre-PhoS was accumulated both in the inner membrane and in the cytoplasm. The cytoplasmic pre-PhoS could not be exported post-translationally; only the membrane-associated precursor could be matured and exported. Preliminary evidence has been obtained for the existence of a translation stop. The pause site in pre-PhoS mRNA translation occurs when 70 to 80 amino acids have been assembled, and appears to be related to the coupling of synthesis and export.
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Lazdunski
D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000096:biosynthesis; D004926:Escherichia coli / Q000378:metabolism*; D028044:Phosphate-Binding Proteins; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000235:genetics; D011499:Protein Processing, Post-Translational; D012329:RNA, Bacterial / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism
D001426:Bacterial Proteins; D002352:Carrier Proteins; D028044:Phosphate-Binding Proteins; D011498:Protein Precursors; D012329:RNA, Bacterial; D012333:RNA, Messenger