Isolation, characterisation and expression of the bacterioferritin gene of Rhodobacter capsulatus.
The nucleotide sequence of the Rhodobacter capsulatus bacterioferritin gene (bfr) was determined and found to encode a protein of 161 amino acids with a predicted molecular mass of 18,174 Da. The molecular mass of the purified protein was estimated to be 18,176. +/ 0.80 Da by electrospray mass spectrometry. The bfr was introduced into an expression vector, and bacterioferritin was produced to a high level in Escherichia coli. The amino acids which are involved in haem ligation, and those provide ligands in the binuclear metal centre in bacterioferritin from E. coli are conversed in the R. capsulatus protein. The sequences of bacterioferritins, ferritin-like proteins, and proteins similar to Dps of E. coli are compared, and membership of the bacterioferritin family re-evaluated.
Penfold
C N
CN
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich, UK.
Ringeling
P L
PL
Davy
S L
SL
Moore
G R
GR
McEwan
A G
AG
Spiro
S
S
D001426:Bacterial Proteins; D001483:Base Sequence; D003573:Cytochrome b Group / Q000235:genetics*; D005293:Ferritins / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics; D007501:Iron / Q000378:metabolism; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D016354:Rhodobacter capsulatus / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D005293:Ferritins; C018032:bacterioferritin; D007501:Iron