Physical, chemical and immunological properties of the bacterioferritins of Escherichia coli, Pseudomonas aeruginosa and Azotobacter vinelandii.
The 70-amino-acid-residue N-terminal sequence of the bacterioferritin (BFR) of Azotobacter vinelandii was determined and shown to be highly similar to the N-terminal sequences of the Escherichia coli and Nitrobacter winogradskyi bacterioferritins. Electrophoretic and immunological analyses further indicate that the bacterioferritins of E. coli, A. vinelandii and Pseudomonas aeruginosa are closely related. A novel, two-subunit assembly state that predominates over the 24-subunit form of BFR at low pH was demonstrated. The results indicate that the bacterioferritins form a family of proteins that are distinct from the ferritins of plants and animals.
Andrews
S C
SC
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, U.K.
Findlay
J B
JB
Guest
J R
JR
Harrison
P M
PM
Keen
J N
JN
Smith
J M
JM
D000595:Amino Acid Sequence; D001395:Azotobacter / Q000032:analysis*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000276:immunology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003429:Cross Reactions; D003573:Cytochrome b Group / Q000737:chemistry* / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000032:analysis*; D005293:Ferritins / Q000737:chemistry* / Q000276:immunology; D005779:Immunodiffusion / Q000379:methods; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D009576:Nitrobacter / Q000032:analysis*; D011550:Pseudomonas aeruginosa / Q000032:analysis*; D013045:Species Specificity
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D005293:Ferritins; C018032:bacterioferritin