start-ver=1.4
cd-journal=joma
no-vol=15
cd-vols=
no-issue=3
article-no=
start-page=403
end-page=410
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2011
dt-pub=201105
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Characterization of an OmpA-like outer membrane protein of the acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidans
en-subtitle=
kn-subtitle=
en-abstract=
kn-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.
en-copyright=
kn-copyright=

en-aut-name=ManchurMohammed Abul
en-aut-sei=Manchur
en-aut-mei=Mohammed Abul
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=KikumotoMei
en-aut-sei=Kikumoto
en-aut-mei=Mei
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=KanaoTadayoshi
en-aut-sei=Kanao
en-aut-mei=Tadayoshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=TakadaJun
en-aut-sei=Takada
en-aut-mei=Jun
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

en-aut-name=KamimuraKazuo
en-aut-sei=Kamimura
en-aut-mei=Kazuo
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=5
ORCID=

affil-num=1
en-affil=
kn-affil=Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University

affil-num=2
en-affil=
kn-affil=Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University

affil-num=3
en-affil=
kn-affil=Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University

affil-num=4
en-affil=
kn-affil=Division of Chemical and Biological Technology, Graduate School of Natural Science and Technology, Okayama University

affil-num=5
en-affil=
kn-affil=Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
en-keyword=Acidithiobacillus ferrooxidans
kn-keyword=Acidithiobacillus ferrooxidans
en-keyword=Iron-oxidizing bacterium
kn-keyword=Iron-oxidizing bacterium
en-keyword=Acidophile
kn-keyword=Acidophile
en-keyword=Outer membrane protein
kn-keyword=Outer membrane protein
en-keyword=OmpA
kn-keyword=OmpA
END