1985
DOI: 10.1128/jb.162.3.972-978.1985
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Defective secretion of maltose- and ribose-binding proteins caused by a truncated periplasmic protein in Escherichia coli

Abstract: The secretion in Escherichia coli of a C-terminally truncated periplasmic enzyme from Salmonella typhimurium, the glpQ-encoded glycerolphosphate phosphodiesterase, was studied. Plasmid pRH100, carrying the truncated glpQ gene, directs the synthesis of a 30,000-molecular-weight (30 K) protein that is processed to a mature 27.5 K protein. (The mature wild-type protein is a 38 K protein.) The truncated protein is not released into the periplasm but remains membrane associated, although it becomes protease sensiti… Show more

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Cited by 28 publications
(1 citation statement)
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“…A short C-terminal deletion has been reported to shift the E. coli 13-lactamase from the periplasm to the membrane (43). While similar findings with the maltose-binding protein were thought to reflect attachment of aggregated protein to the membrane, rather than retention in the membrane (40), a truncated glycerophosphate phosphodiesterase seems definitely to be shifted from periplasm to membrane, since it interferes with the secretion of other periplasmic proteins (34). In such studies, it would be of interest to test for effects not only on protein export, but also on the integrity of the osmotic barrier.…”
Section: Mechanistic Challengesmentioning
confidence: 88%
“…A short C-terminal deletion has been reported to shift the E. coli 13-lactamase from the periplasm to the membrane (43). While similar findings with the maltose-binding protein were thought to reflect attachment of aggregated protein to the membrane, rather than retention in the membrane (40), a truncated glycerophosphate phosphodiesterase seems definitely to be shifted from periplasm to membrane, since it interferes with the secretion of other periplasmic proteins (34). In such studies, it would be of interest to test for effects not only on protein export, but also on the integrity of the osmotic barrier.…”
Section: Mechanistic Challengesmentioning
confidence: 88%