ID | 46844 |
FullText URL | |
Author |
Manchur, Mohammed Abul
Kikumoto, Mei
Kamimura, Kazuo
Kaken ID
researchmap
|
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 |
English
|
Copyright Holders | © The Author(s) 2011. This article is published with open access at Springerlink.com
|
File Version | publisher
|
Refereed |
True
|
DOI | |
PubMed ID | |
Web of Science KeyUT |