Artificial insertion of peptides between signal peptide and mature protein: effect on secretion and processing of hybrid thermostable alpha-amylases in Bacillus subtilis and Escherichia coli cells

Journal of General Microbiology
Y ItohK Yamane

Abstract

To study the effect of inserted peptides on the secretion and processing of exported proteins in Bacillus subtilis and Escherichia coli, pBR322-derived DNA fragments coding for small peptides were inserted between the DNA coding for the 31 amino acid B. subtilis alpha-amylase signal peptide and that coding for the mature part of the extracellular thermostable alpha-amylase of B. stearothermophilus. Most of the inserted peptides (21 to 65 amino acids) decreased the production of the enzyme in B. subtilis and E. coli, the effect of each peptide being similar in the two strains. In contrast, with one peptide (a 21 amino acid sequence encoded by the extra DNA in pTUBE638), the production of alpha-amylase was enhanced more than 1.7-fold in B. subtilis in comparison with that of the parent strain. The molecular masses of the thermostable alpha-amylases in the periplasm of the E. coli transformants varied for each peptide insert, whereas those in the culture supernatants of the B. subtilis transformants had molecular masses similar to that of the mature enzyme. Based on the NH2-terminal amino acid sequence of the hybrid protein from pTUBE638, it was shown that in E. coli, the NH2-terminally extended thermostable alpha-amylase was tran...Continue Reading

Citations

Mar 27, 2013·Applied Microbiology and Biotechnology·Kheng Oon LowRosli Md Illias
Mar 1, 1996·Applied Microbiology and Biotechnology·V A Hale, J L Schottel
Nov 18, 2004·Biochimica Et Biophysica Acta·Matti SarvasJan Maarten van Dijl
Mar 1, 1991·Xenobiotica; the Fate of Foreign Compounds in Biological Systems·J MolnárF Gutmann
Oct 26, 2001·Protein Expression and Purification·K J Jeong, S Y Lee
Mar 1, 1993·Microbiological Reviews·M Simonen, I Palva

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