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. 1987 Dec;84(23):8540–8543. doi: 10.1073/pnas.84.23.8540

Substitution of tyrosine for either cysteine in beta-lactamase prevents release from the membrane during secretion.

R Fitts 1, Z Reuveny 1, J van Amsterdam 1, J Mulholland 1, D Botstein 1
PMCID: PMC299580  PMID: 3317414

Abstract

Six independent secretion-defective mutations were found that result in failure to release protein from the membrane into the periplasmic space of Salmonella typhimurium after removal of the signal peptide. The mutant protein is found in a membrane-bound form accessible to trypsin added to intact spheroplasts. The phenotype of these mutations supports the existence in general of an intermediate in bacterial secretion. All six mutations changed one or the other of the two cysteine residues in the mature protein to tyrosine, suggesting that these residues are involved in the release of protein into the periplasmic space, most likely by affecting protein folding.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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