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ID 46844
フルテキストURL
著者
Manchur, Mohammed Abul Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
Kikumoto, Mei Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
Kanao, Tadayoshi Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
Takada, Jun Division of Chemical and Biological Technology, Graduate School of Natural Science and Technology, Okayama University
Kamimura, Kazuo Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
抄録
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.
キーワード
Acidithiobacillus ferrooxidans
Iron-oxidizing bacterium
Acidophile
Outer membrane protein
OmpA
発行日
2011-05
出版物タイトル
Extemophiles
15巻
3号
出版者
Springer Japan
開始ページ
403
終了ページ
410
ISSN
1431-0651
NCID
AA11156867
資料タイプ
学術雑誌論文
言語
English
著作権者
© The Author(s) 2011. This article is published with open access at Springerlink.com
論文のバージョン
publisher
査読
有り
DOI
PubMed ID
Web of Sience KeyUT