A short N-proximal region of prochymosin inhibits the secretion of hybrid proteins from Escherichia coli

Little, Stephen F.; Campbell, Callum J.; Evans, Ian J.; Hayward, E.C.; Lilley, R.; Robinson, Martyn K.

doi:10.1016/0378-1119(89)90118-2

Cited by 15 publications

(3 citation statements)

References 17 publications

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“…It was thought that this "shotgun approach" would induce a whole variety of chaperones, including yet undiscovered periplasmic ones (581). It is now clear that besides the signal peptide, other structural features in proteins are involved in membrane transport (55,87,108,333,346,356,466,542).…”

Section: Periplasmic Expressionmentioning

confidence: 99%

Strategies for achieving high-level expression of genes in Escherichia coli.

Makrides¹

1996

Microbiological Reviews

782

388

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Section: Periplasmic Expressionmentioning

confidence: 99%

Strategies for achieving high-level expression of genes in Escherichia coli.

Makrides¹

1996

Microbiological Reviews

782

388

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“…Therefore, BRP-mediated release was not further investigated. It has been reported that a region in the amino-terminus of bovine prochymosin prevents processing and secretion by E. coli (Little et al, 1989). In contrast, efficient signal peptide directed secretion of prochymosin has been achieved in yeasts and fungi (Tsuchiya et al, 1993;Van den Bergh et al, 1990).…”

Section: Subcellular Localization Of Ot-galactosidase Prochymosin Amentioning

confidence: 99%

Application of the pCloDF13 bacteriocin release protein in the release of heterologous proteins by Escherichia coli : Production of plant α-galactosidase

et al. 1995

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The bacteriocin release protein (BRP) mediated release of several eukaryotic proteins was studied in Escherichia coli. The genes for the plant proteins ct-galactosidase and thaumatin, and for the mammalian proteins prochymosine and prophospholipase A2, were cloned behind the OmpA signal peptide. The tx-galactosidase was expressed and secreted into the periplasm. Prochymosine and thaumatin were poorly expressed. Release experiments showed that about 5 mg/l of tx-galactosidase was excreted into the extracellular medium upon induction of the BRP.

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“…In addition, the mammalian protein prochymosin was found extracellularly when fused to the hemolysin secretion signal [135]. This is interesting because it has been shown that signal peptide directed translocation of prochymosin across the cytoplasmic membrane is not possible in E. coli [136].…”

Section: Secretion Of Heterologous Proteins By E Colimentioning

confidence: 99%

Bacteriocin release proteins: mode of action, structure, and biotechnological application

Wal

Luirink

Oudega

1995

FEMS Microbiology Reviews

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The mechanism by which Gram-negative bacteria like Escherichia coli secrete bacteriocins into the culture medium is unique and quite different from the mechanism by which other proteins are translocated across the two bacterial membranes, namely through the known branches of the general secretory pathway. The release of bacteriocins requires the expression and activity of a so-called bacteriocin release protein and the presence of the detergent-resistant phospholipase A in the outer membrane. The bacteriocin release proteins are highly expressed small lipoproteins which are synthesized with a signal peptide that remains stable and which accumulates in the cytoplasmic membrane after cleavage. The combined action of these stable, accumulated signal peptides, the lipid-modified mature bacteriocin release proteins (BRPs) and phospholipase A cause the release of bacteriocins. The structure and mode of action of these BRPs as well as their application in the release of heterologous proteins by E. coli is described in this review.

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A short N-proximal region of prochymosin inhibits the secretion of hybrid proteins from Escherichia coli

Cited by 15 publications

References 17 publications

Strategies for achieving high-level expression of genes in Escherichia coli.

Strategies for achieving high-level expression of genes in Escherichia coli.

Application of the pCloDF13 bacteriocin release protein in the release of heterologous proteins by Escherichia coli : Production of plant α-galactosidase

Bacteriocin release proteins: mode of action, structure, and biotechnological application

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