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Gene. 1991 Jun 30;102(2):277-82.

Optimization of the signal-sequence cleavage site for secretion from Bacillus subtilis of a 34-amino acid fragment of human parathyroid hormone.

Author information

1
Corporate Research Division, Procter and Gamble Company, Cincinnati, OH 45239-8707.

Abstract

We have effected the secretion from Bacillus subtilis of a 34-amino acid (aa) fragment of human parathyroid hormone (PTH,1-34), using a Bacillus amyloliquefaciens neutral protease signal sequence. The secretion efficiency depended on the aa sequence near the signal-sequence cleavage site. We constructed a series of gene fusions encoding different pairs of aa between the signal sequence and PTH,1-34. There was a correlation between those polypeptides which were efficiently secreted and the potential for a beta-turn in the region just beyond the signal-sequence cleavage site. Based on this correlation, we constructed a gene fusion which specified Gly rather than Ala at the C terminus of the signal sequence, thus creating a beta-turn potential at the end of the signal sequence. The change provided a slight increase in secretion efficiency.

PMID:
1908402
DOI:
10.1016/0378-1119(91)90090-x
[Indexed for MEDLINE]

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