Two hih-affinity iron uptake systems are known in Salmonella typhunurinum, one utiig iron-enteohelin and the other uliing ferichrome. It has been shown previously that expreon of several element of the iron-enterochelin uptake system are ated by the iron content of the medium, with growth in high-iron medium resulting in repon of enzymes of enterochelin synthsis and degradation and of the ability of whole cels to take up iron-enterochelin In this study we describe a mutant strain in which growth in high-iron medium was assciated with constitutive exreon of. (i) iron-enterochelin uptake by whole cells (ii) ferirome uptake by whole cells; (iii) synthesis of enterochelin; (iv) itracellular degradation of iron-enterochelin; and (v) synthesis of three major outer-membe prot (OM1, OM2, and OM3). In conbwtr in the wildtype strain the4s prorties were only after growth in iron-deficient medium. It is proposed that the mutation ffects a gene responsible for regulating expssion of the structual genes for the components of the high-affinity iron uptake ystems. The term fur, for iron (Fe) uptake regulation, is suggetd for this new class of mutant. Several high-affinity systems are known to perticipate in iron uptake in SabnoneUa typhimurinum and Ewcherichia coli. The enterochelin uptake system facilitates entry of iron complexed to enterochelin, a cyclic trimer of 2,3dihydroxybenzoylserine syntheized and excreted by the bacterium itself. This presumably represents the physiologically relevant system under most circunutances (3, 31). The fernchrome uptake system facilitates entry of iron complexed to siderophores produced by fimgi (3, 19, 23). A third high-affinity uptake systm facilitats entry ofiron-citrate complexes in E. coli but is not present in S. typhimurium (8, 32).