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

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

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 constru...

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Bibliographic Details
Published in:Gene Vol. 102; no. 2; p. 277
Main Authors: Saunders, C W, Pedroni, J A, Monahan, P M
Format: Journal Article
Language:English
Published: Netherlands 30-06-1991
Subjects:
Amino Acid Sequence
Bacillus subtilis - genetics
Bacillus subtilis - metabolism
Base Sequence
DNA
Humans
Molecular Sequence Data
Mutation
Parathyroid Hormone - genetics
Parathyroid Hormone - metabolism
Protein Conformation
Protein Processing, Post-Translational
Protein Sorting Signals - genetics
Protein Sorting Signals - metabolism
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Regulatory Sequences, Nucleic Acid
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Summary: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.
ISSN:0378-1119
DOI:10.1016/0378-1119(91)90090-X