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PMID: 3110129 Published · ppublish English Journal Article

Secretion of human serum albumin from Bacillus subtilis.

Journal of bacteriology ·Vol. 169 ·No. 7 ·1987-07-00 ·Pages 2917-25

Saunders CW, Schmidt BJ, Mallonee RL, Guyer MS

Abstract

We have fused the structural gene (hsa) for human serum albumin (HSA) to the expression elements and signal sequence coding region of each of two genes from Bacillus amyloliquefaciens P, an alpha-amylase gene (amyBamP) and a neutral protease gene (nprBamP). Bacillus subtilis strains harboring either of these gene fusions synthesized a protein with the antigenic characteristics and size (68 kilodaltons) of HSA. Results from pulse-labeling studies indicated that the bacterially produced HSA was secreted from cells which had been converted to protoplasts. Results from similar studies with intact cells suggested that the signal sequence was removed from the hybrid protein, providing further evidence that B. subtilis can translocate this foreign protein across the cell membrane. Signal sequence removal was efficient when the level of HSA synthesis was low. However, in strains which synthesized HSA at a high level, signal sequence removal was less efficient.

MeSH Terms
Bacillus subtilis/physiology Biological Transport Cell Membrane/metabolism Protein Processing, Post-Translational Protein Sorting Signals/genetics Recombinant Fusion Proteins/metabolism Recombinant Proteins/metabolism Serum Albumin/biosynthesis,metabolism
Chemicals
Protein Sorting Signals Recombinant Fusion Proteins Recombinant Proteins Serum Albumin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Saunders C W
Schmidt B J
Mallonee R L
Guyer M S
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36 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1987-07-00
Pages
2917-25
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC212327
Subset
IM
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