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Effects of signal peptide mutations on processing of Bacillus stearothermophilus α-amylase in Escherichia coli

Suominen, I.; Meyer, P. LU ; Tilgmann, C. LU ; Glumoff, T.; Glumoff, V.; Kapyla, J. and Mantsala, P. (1995) In Microbiology 141(3). p.649-654
Abstract

Bacillus stearothermophilus α-amylase has a signal peptide typical for proteins exported by Gram-positive bacteria. There is only one signal peptidase processing site when the protein is exported from the original host, but when it is exported by Escherichia coli, two alternative sites are utilized. Site-directed mutagenesis was used to study the processing in E. coli. Processing sites for 13 B. stearothermophilus α-amylases carrying mutations in their signal peptide were determined. Processing of the signal peptide was remarkably tolerant to mutations, because switching between the alternative sites was possible. The length and the sequence of the region between the hydrophobic core and the cleavage site was crucial for determining the... (More)

Bacillus stearothermophilus α-amylase has a signal peptide typical for proteins exported by Gram-positive bacteria. There is only one signal peptidase processing site when the protein is exported from the original host, but when it is exported by Escherichia coli, two alternative sites are utilized. Site-directed mutagenesis was used to study the processing in E. coli. Processing sites for 13 B. stearothermophilus α-amylases carrying mutations in their signal peptide were determined. Processing of the signal peptide was remarkably tolerant to mutations, because switching between the alternative sites was possible. The length and the sequence of the region between the hydrophobic core and the cleavage site was crucial for determining the choice of the processing site. Some mutations more distal to the cleavage site also affected the site preference.

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author
publishing date
type
Contribution to journal
publication status
published
keywords
α-amylase, Processing, Protein secretion, Signal peptidase, Signal peptide
in
Microbiology
volume
141
issue
3
pages
6 pages
publisher
MAIK Nauka/Interperiodica
external identifiers
  • Scopus:0028957251
ISSN
1350-0872
language
English
LU publication?
no
id
0e46da1f-6f6c-4cd3-8b39-ed1d054d222a
date added to LUP
2016-04-11 13:19:57
date last changed
2016-06-29 09:03:34
@misc{0e46da1f-6f6c-4cd3-8b39-ed1d054d222a,
  abstract     = {<p>Bacillus stearothermophilus α-amylase has a signal peptide typical for proteins exported by Gram-positive bacteria. There is only one signal peptidase processing site when the protein is exported from the original host, but when it is exported by Escherichia coli, two alternative sites are utilized. Site-directed mutagenesis was used to study the processing in E. coli. Processing sites for 13 B. stearothermophilus α-amylases carrying mutations in their signal peptide were determined. Processing of the signal peptide was remarkably tolerant to mutations, because switching between the alternative sites was possible. The length and the sequence of the region between the hydrophobic core and the cleavage site was crucial for determining the choice of the processing site. Some mutations more distal to the cleavage site also affected the site preference.</p>},
  author       = {Suominen, I. and Meyer, P. and Tilgmann, C. and Glumoff, T. and Glumoff, V. and Kapyla, J. and Mantsala, P.},
  issn         = {1350-0872},
  keyword      = {α-amylase,Processing,Protein secretion,Signal peptidase,Signal peptide},
  language     = {eng},
  number       = {3},
  pages        = {649--654},
  publisher    = {ARRAY(0x9697da8)},
  series       = {Microbiology},
  title        = {Effects of signal peptide mutations on processing of Bacillus stearothermophilus α-amylase in Escherichia coli},
  volume       = {141},
  year         = {1995},
}