The iron storage protein, ferritin, plays a key role in iron metabolism. Its ability to sequester
the element gives ferritin the dual functions of iron detoxification and iron reserve. The …

Abstract Dating from the Pre-Cambrian era, cyanobacteria have a long history of adaptation
to the Earth's environment. By evolving oxygen via photosynthetic reactions similar to those …

A small RNA, RyhB, was found as part of a genomewide search for novel small RNAs in
Escherichia coli. The RyhB 90-nt RNA down-regulates a set of iron-storage and iron-using …

Three native E. coli proteins—NusA, GrpE, and bacterioferritin (BFR)—were studied in
fusion proteins expressed in E. coli for their ability to confer solubility on a target insoluble …

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 …

The Escherichia coli Fur protein, with its iron (II) cofactor, represses iron assimilation and
manganese superoxide dismutase (MnSOD) genes, thus coupling iron metabolism to …

The NifS and NifU proteins from Azotobacter vinelandii are required for the full activation of
nitrogenase. NifS is a homodimeric cysteine desulfurase that supplies the inorganic sulfide …

The Pseudomonas aeruginosa genes pilB‐D and pilQ are necessary for the assembly of
type 4 fimbriae. Homologues of these genes and of the subunit (pilin) gene have been …

Escherichia coli contains at least two iron storage proteins, a ferritin (FtnA) and a
bacterioferritin (Bfr). To investigate their specific functions, the corresponding genes (ftnA …

In this work, we characterize genes in Mycobacterium tuberculosis that are regulated by
IdeR (i ron‐de pendent r egulator), an iron‐responsive DNA‐binding protein of the DtxR …