Iron storage in bacteria.
Iron is an essential nutrient for nearly all organisms but presents problems of toxicity, poor solubility and low availability. These problems are alleviated through the use of iron-storage proteins. Bacteria possess two types of iron-storage protein, the haem-containing bacterioferritins and the haem-free ferritins. These proteins are widespread in bacteria, with at least 39 examples known so far in eubacteria and archaebacteria. The bacterioferritins and ferritins are distantly related but retain similar structural and functional properties. Both are composed of 24 identical or similar subunits (approximately 19 kDa) that form a roughly spherical protein (approximately 450 kDa, approximately 120 A diameter) containing a large hollow centre (approximately 80 A diameter). The hollow centre acts as an iron-storage cavity with the capacity to accommodate at least 2000 iron atoms in the form of a ferric-hydroxyphosphate core. Each subunit contains a four-helix bundle which carries the active site or ferroxidase centre of the protein. The ferroxidase centres endow ferrous-iron-oxidizing activity and are able to form a di-iron species that is an intermediate in the iron uptake, oxidation and core formation process. Bacterioferritins contain up to 12 protoporphyrin IX haem groups located at the two-fold interfaces between pairs of two-fold related subunits. The role of the haem is unknown, although it may be involved in mediating iron-core reduction and iron release. Some bacterioferritins are composed of two subunit types, one conferring haem-binding ability (alpha) and the other (beta) bestowing ferroxidase activity. Bacterioferritin genes are often adjacent to genes encoding a small [2Fe-2S]-ferredoxin (bacterioferritin-associated ferredoxin or Bfd). Bfd may directly interact with bacterioferritin and could be involved in releasing iron from (or delivering iron to) bacterioferritin or other iron complexes. Some bacteria contain two bacterioferritin subunits, or two ferritin subunits, that in most cases co-assemble. Others possess both a bacterioferritin and a ferritin, while some appear to lack any type of iron-storage protein. The reason for these differences is not understood. Studies on ferritin mutants have shown that ferritin enhances growth during iron starvation and is also involved in iron accumulation in the stationary phase of growth. The ferritin of Campylobacter jejuni is involved in redox stress resistance, although this does not appear to be the case for Escherichia coli ferritin (FtnA). No phenotype has been determined for E. coli bacterioferritin mutants and the precise role of bacterioferritin in E. coli remains uncertain.
Andrews
S C
SC
School of Animal and Microbial Sciences, University of Reading, UK.
D001426:Bacterial Proteins / Q000378:metabolism / Q000502:physiology; D016123:Campylobacter jejuni / Q000378:metabolism / Q000502:physiology; D003573:Cytochrome b Group / Q000378:metabolism / Q000502:physiology*; D004926:Escherichia coli / Q000378:metabolism / Q000502:physiology*; D005288:Ferredoxins / Q000378:metabolism / Q000502:physiology; D005293:Ferritins / Q000378:metabolism / Q000502:physiology*; D015964:Gene Expression Regulation, Bacterial; D006418:Heme / Q000378:metabolism; D006422:Hemerythrin; D012416:Rubredoxins; D013329:Structure-Activity Relationship; D013482:Superoxide Dismutase / Q000378:metabolism / Q000502:physiology
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D005288:Ferredoxins; D006422:Hemerythrin; D012416:Rubredoxins; C055857:rubrerythrins; D006418:Heme; D005293:Ferritins; C018032:bacterioferritin; D013482:Superoxide Dismutase