Dehydrins are a family of desiccation proteins that were identified originally in plants (T.J. Close, A.A. Kortt, P.M. Chandler [1989] Plant Mol Biol 13: 95-108; G. Galau, T.J. Close [1992] Plant Physiol 98: 1523-1525). Dehydrins are characterized by the consensus amino acid sequence domain EKKGIMDKIKEKLPG found at or near the carboxy terminus; the core of this domain (KIKEKLPG) may be repeated from one to many times within the complete polypeptide. Dehydrins generally accumulate in plants in response to dehydration stress, regardless of whether the stimulus is evaporation, chilling, or a decrease in external osmotic potential. Polyclonal antibodies highly specific to the consensus carboxy terminus of plant dehydrins were used to search for dehydrins in cyanobacteria, many of which are known to survive desiccation. A 40-kD osmotic-stress-induced protein was identified in Anabaena sp. strain PCC 7120. The 40-kD protein was usually not detected in logarithmic cultures and was induced by shifting the growth medium to higher solute concentrations. Several solutes have inductive effects, including sucrose, sorbitol, and polyethylene glycol (PEG). Measurements of osmotic potential suggest that a shift of -0.5 MPa (sucrose and PEG) or -1.2 MPa (sorbitol) is sufficient to induce synthesis of the 40-kD protein. Glycerol, which is highly permeable, was not an inducer at -1.2 MPa (0.5 M), nor was the plant hormone abscisic acid. Induction appears to be evoked by a shift in osmotic potential approximately equal in absolute magnitude to the expected turgor pressure of bacterial cells in logarithmic phase growth. A dehydrin-like polypeptide was also identified among osmotically induced proteins from two other filamentous, heterocyst-forming cyano-bacteria. A 40-kD protein was observed in Calothrix sp. strain PCC 7601, and in Nostoc sp. strain Mac-R2, an osmotic-induced doublet at 39 and 40 kD was observed. From these data, it appears that cyanobacteria produce a dehydrin-like protein under osmotic stress.