Streptomyces coelicolor contains paralogous versions of seven ribosomal proteins (S14, S18, L28, L31, L32, L33, and L36), which differ in their potential to bind structural zinc. The paralogues are termed C ؉ or C ؊ on the basis of the presence or absence of putative cysteine ligands. Here, mutational studies suggest that the C ؊ version of L31 can functionally replace its C ؉ paralogue only when expressed at an artificially elevated level. We show that the level of expression of four transcriptional units encoding C ؊ proteins is elevated under conditions of zinc deprivation. Zur controls the expression of three transcriptional units (including rpmG2, rpmE2, rpmB2, rpsN2, rpmF2, and possibly rpsR2). Zur also controls the expression of the znuACB operon, which is predicted to encode a high-affinity zinc transport system. Surprisingly, the zinc-responsive control of the rpmG3-rpmJ2 operon is dictated by R , a sigma factor that was previously shown to control the response to disulfide stress in S. coelicolor. The induction of R activity during zinc limitation establishes an important link between thiol-disulfide metabolism and zinc homeostasis.Bacterial 70S ribosomes are assembled on mRNA from 30S and 50S subunits during the process of translation initiation. The ribosome is approximately two-thirds RNA and one-third protein. The 30S subunit usually contains 21 proteins and 16S rRNA, whereas the 50S subunit comprises up to 36 proteins together with 23S and 5S rRNA. A major role of ribosomal proteins (R proteins) is to stabilize the rRNA (31), although several proteins play additional roles in ribosome function (8).