Secretion of Bacillus subtilis α-amylase in the periplasmic space of Escherichia coli

K. I. Tachibana, K. Yoda, S. Watanabe, H. Kadokura, Y. Katayama, K. Yamane, M. Yamasaki, G. Tamura

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

The Bacillus subtilis α-amylase structural gene (amyE) lacking its own signal peptide coding sequence was joined to the end of the Escherichia coli alkaline phosphatase (phoA) signal peptide coding sequence by using the technique of oligonucleotide-directed site-specific deletion. On induction of the phoA promoter, the B. subtilis α-amylase was expressed and almost all the activity was found in the periplasmic space of E. coli. The sequence of the five amino-terminal amino acids of the secreted polypeptide was Glu-Thr-Ala-Asn-Lys-, and thus the fused protein was correctly processed by the E. coli signal peptidase at the end of the phoA signal peptide.

Original languageEnglish
Pages (from-to)1775-1782
Number of pages8
JournalJournal of General Microbiology
Volume133
Issue number7
Publication statusPublished - 1987 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology

Fingerprint

Dive into the research topics of 'Secretion of Bacillus subtilis α-amylase in the periplasmic space of Escherichia coli'. Together they form a unique fingerprint.

Cite this