Salinity-stress-induced proteins in two nitrogen-fixing Anabaena strains differentially tolerant to salt

Apte, S. K. ; Bhagwat, A. A. (1989) Salinity-stress-induced proteins in two nitrogen-fixing Anabaena strains differentially tolerant to salt Journal of Bacteriology, 171 (2). pp. 909-915. ISSN 0021-9193

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Salinity altered the protein synthesis patterns in two cyanobacterial strains: Anabaena torulosa, a salt-tolerant brackish water strain, and Anabaena sp. strain L-31, a salt-sensitive freshwater strain. The cyanobacterial response to salinity was very rapid, varied with time, and was found to be correlated with the external salt (NaCl) concentration during stress. Salinity induced three prominent types of modification. First, the synthesis of several proteins was inhibited, especially in the salt-sensitive strain; second, the synthesis of certain proteins was significantly enhanced; and third, synthesis of a specific set of proteins was induced de novo by salinity stress. Proteins which were selectively synthesized or induced de novo during salt stress, tentatively called the salt-stress proteins, were confined to an isoelectric pI range of 5.8 to 7.5 and were distributed in a molecular mass range of 12 to 155 kilodaltons. These salt-stress proteins were unique to each Anabaena strain, and their expression was apparently regulated coordinately during exposure to salt stress. In Anabaena sp. strain L-31, most of the salt-stress-induced proteins were transient in nature and were located mainly in the cytoplasm. In A. torulosa, salt-stress-induced proteins were evenly distributed in the membrane and cytoplasmic fractions and were persistent, being synthesized at high rates throughout the period of salinity stress. These initial studies reveal that salinity-induced modification of protein synthesis, as has been demonstrated in higher plant species, also occurs in cyanobacteria and that at least some of the proteins preferentially synthesized during salt stress may be important to cyanobacterial osmotic adaptation.

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