A sulfur-regulated gene (cysA) that encodes the membrane-associated ATP-binding protein of the sulfate transport system of the cyanobacterium Synechococcus sp. strain PCC 7942 was recently isolated and sequenced. Adjacent to cysA and transcribed in the opposite direction is a gene encoding the sulfate-binding protein (sbpA Cyanobacteria are obligate photoautotrophs that undergo a complex set of distinct morphological and physiological changes when deprived of macronutrients such as sulfur and nitrogen. A visually dramatic response to nutrient deprivation is the degradation of the light-harvesting complex, the phycobilisome, and the concomitant decline in the levels of phycocyanin and allophycocyanin. Additionally, there is a decrease in chlorophyll levels and attenuation of the photosynthetic membranes (44, 60). Other changes that accompany nutrient deprivation include cell wall thickening (25) and the accumulation of electron-opaque inclusion bodies in the cytoplasm of the cell (31, 60).In addition to the general responses described above, cyanobacteria exhibit specific responses when deprived of a given nutrient. During growth in sulfur-deficient medium, the unicellular cyanobacterium Anacystis nidulans and the closely related Synechococcus sp. strain PCC 7942 display an increased rate of sulfate transport (15,24 In the enteric bacteria Salmonella typhimurium and Escherichia coli, sulfate transport is accomplished by a single active uptake system. This permease complex is composed of three cytoplasmic membrane components and a substratespecific binding protein located in the periplasmic space (3, 28). The sulfate-binding protein of S. typhimurium has been isolated and sequenced and its crystal structure has been resolved (23,36,40). It is present in the periplasmic space at very high levels and binds one sulfate molecule per molecule of protein. Two of the cytoplasmic membrane proteins appear to span the lipid bilayer and may form a channel for the passage of the substrate. A third membrane protein hydrolyzes ATP to provide the energy required for concentrating the substrate inside the cell (4).Much of the information on sulfate uptake in enteric bacteria has accrued from studies of cysteine auxotrophs. Mutations that block sulfate transport map to the cysA locus; all three cistrons in this locus are required for normal uptake (34,35 In this communication, we present a characterization of the region of DNA adjacent to cysA and conclude that it encodes the remaining components of the sulfate permease. These conclusions are based on homology to analogous polypeptides from both the sulfate permease system of S. typhimurium and E. coli and the phenotype of mutant strains