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ID 46844
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Author
Manchur, Mohammed Abul
Kikumoto, Mei
Abstract
An OmpA family protein (FopA) previously reported as one of the major outer membrane proteins of an acidophilic iron-oxidizing bacterium Acidithiobacillus ferrooxidans was characterized with emphasis on the modification by heat and the interaction with peptidoglycan. A 30-kDa band corresponding to the FopA protein was detected in outer membrane proteins extracted at 75A degrees C or heated to 100A degrees C for 10 min prior to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). However, the band was not detected in outer membrane proteins extracted at a parts per thousand currency sign40A degrees C and without boiling prior to electrophoresis. By Western blot analysis using the polyclonal antibody against the recombinant FopA, FopA was detected as bands with apparent molecular masses of 30 and 90 kDa, suggesting that FopA existed as an oligomeric form in the outer membrane of A. ferrooxidans. Although the fopA gene with a sequence encoding the signal peptide was successfully expressed in the outer membrane of Escherichia coli, the recombinant FopA existed as a monomer in the outer membrane of E. coli. FopA was detected in peptidoglycan-associated proteins from A. ferrooxidans. The recombinant FopA also showed the peptidoglycan-binding activity.
Keywords
Acidithiobacillus ferrooxidans
Iron-oxidizing bacterium
Acidophile
Outer membrane protein
OmpA
Published Date
2011-05
Publication Title
Extemophiles
Volume
volume15
Issue
issue3
Publisher
Springer Japan
Start Page
403
End Page
410
ISSN
1431-0651
NCID
AA11156867
Content Type
Journal Article
language
英語
Copyright Holders
© The Author(s) 2011. This article is published with open access at Springerlink.com
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Refereed
True
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