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Suppression of growth defects of α-amylase secreting Escherichia coli by signal sequence fusion

Suominen, Ilari; Käpylä, Jarmo; Tilgmann, Carola LU ; Glumoff, Virpi and Mäntsälä, Pekka (1988) In FEMS Microbiology Letters 55(1). p.3-7
Abstract

Two fusions of the Bacillus stearothermophilus α-amylase gene (amyS) with lacpoZ′ were constructed. The first, being a transcriptional fusion, placed amyS directly under lac promoter control eliminating interference by the endogenous promoter. IPTG induction of amyS transcription in this construction resulted in liberation of periplasmic proteins and eventually cell lysis. The other fusion replaced eight N-terminal amino acid residues from the signal sequence by 11 residues from the lacZ′ moiety in pUC-18. Translation initiation signals were also replaced by those from lacpoZ′. In this case IPTG induction resulted in secretion of approx. 35% of total α-amylase activity in the growth medium after 24 h growth without detectable cell... (More)

Two fusions of the Bacillus stearothermophilus α-amylase gene (amyS) with lacpoZ′ were constructed. The first, being a transcriptional fusion, placed amyS directly under lac promoter control eliminating interference by the endogenous promoter. IPTG induction of amyS transcription in this construction resulted in liberation of periplasmic proteins and eventually cell lysis. The other fusion replaced eight N-terminal amino acid residues from the signal sequence by 11 residues from the lacZ′ moiety in pUC-18. Translation initiation signals were also replaced by those from lacpoZ′. In this case IPTG induction resulted in secretion of approx. 35% of total α-amylase activity in the growth medium after 24 h growth without detectable cell lysis. © 1988.

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author
publishing date
type
Contribution to journal
publication status
published
keywords
Bacillus stearothermophilus, Escherichia coli, Periplasmic protein, Protein secretion, α-amylase
in
FEMS Microbiology Letters
volume
55
issue
1
pages
5 pages
publisher
Elsevier
external identifiers
  • Scopus:0023698669
ISSN
0378-1097
language
English
LU publication?
no
id
fa6c734f-1c9a-4ffa-9ea2-51db1c17c6b1
date added to LUP
2016-04-11 13:26:57
date last changed
2016-10-31 09:49:32
@misc{fa6c734f-1c9a-4ffa-9ea2-51db1c17c6b1,
  abstract     = {<p>Two fusions of the Bacillus stearothermophilus α-amylase gene (amyS) with lacpoZ′ were constructed. The first, being a transcriptional fusion, placed amyS directly under lac promoter control eliminating interference by the endogenous promoter. IPTG induction of amyS transcription in this construction resulted in liberation of periplasmic proteins and eventually cell lysis. The other fusion replaced eight N-terminal amino acid residues from the signal sequence by 11 residues from the lacZ′ moiety in pUC-18. Translation initiation signals were also replaced by those from lacpoZ′. In this case IPTG induction resulted in secretion of approx. 35% of total α-amylase activity in the growth medium after 24 h growth without detectable cell lysis. © 1988.</p>},
  author       = {Suominen, Ilari and Käpylä, Jarmo and Tilgmann, Carola and Glumoff, Virpi and Mäntsälä, Pekka},
  issn         = {0378-1097},
  keyword      = {Bacillus stearothermophilus,Escherichia coli,Periplasmic protein,Protein secretion,α-amylase},
  language     = {eng},
  number       = {1},
  pages        = {3--7},
  publisher    = {ARRAY(0x9e1c500)},
  series       = {FEMS Microbiology Letters},
  title        = {Suppression of growth defects of α-amylase secreting Escherichia coli by signal sequence fusion},
  volume       = {55},
  year         = {1988},
}