2001
DOI: 10.1007/s002030100266
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Secretion of human growth hormone by the food-grade bacterium Staphylococcus carnosus requires a propeptide irrespective of the signal peptide used

Abstract: Staphylococcal exoproteins can be divided into two groups. One group comprises proteins bearing only a signal peptide, the other group requires an additional propeptide for secretion. The secretion signals of the propeptide-requiring lipase from Staphylococcus hyicus (Lip) have been frequently used to produce recombinant secretory proteins in the food-grade species Staphylococcus carnosus. However, it has been unclear whether recombinant proteins can be secreted using signal peptides of staphylococcal proteins… Show more

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Cited by 12 publications
(13 citation statements)
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“…Although this has not been previously documented for B. subtilis, there is some precedence for a potential role of pro lip in protein export from the cytoplasm of S. carnosus, and it has been proposed that the pro lip peptide can keep precursor proteins in a translocationcompetent state (50). Whether this is also the case in B. subtilis is worth further investigation.…”
Section: Discussionmentioning
confidence: 84%
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“…Although this has not been previously documented for B. subtilis, there is some precedence for a potential role of pro lip in protein export from the cytoplasm of S. carnosus, and it has been proposed that the pro lip peptide can keep precursor proteins in a translocationcompetent state (50). Whether this is also the case in B. subtilis is worth further investigation.…”
Section: Discussionmentioning
confidence: 84%
“…As a consequence of these disulfide bonds, PhoA has folding requirements that are significantly different from those of proteins that do not contain disulfide bonds, and thus it can act as a model for secretion of heterologous proteins that contain disulfide bonds (23,24). Although use of the prepro-region of the S. hyicus lipase has been described in previous studies (15,18,32,33,45,50), these studies did not include an in-depth examination of the roles of the pre-and pro-regions in the subcellular localization and fate of exported "cargo" proteins like the examination that we performed here for E. coli PhoA using cell fractionation and protease accessibility assays. Several novel and unexpected findings were obtained.…”
Section: Discussionmentioning
confidence: 99%
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“…To address this question, PhoA was fused to the signal peptide (pre lip ) and pro region (pro lip ) of an S. hyicus preprolipase. The combined pre and pro regions are known to act as a productive secretion signal for use in gram-positive bacteria (7,21,22,37), and for efficient secretion of E. coli PhoA by B. subtilis, the preregion alone is insufficient (unpublished observations). The plasmid encoding the resulting hybrid prepro lip -PhoA precursor was designated pPSPhoA5.…”
Section: Resultsmentioning
confidence: 99%