Abstract
We have recently isolated and characterized a 5 S RNA-protein complex (RNP) from the ribosomes of an extreme halophile Halobacterium cu tirubrum [l] . This complex contains two proteins, HL-13 and HL-19, which have been shown to be equivalent to Escherichia coli proteins EL1 8 and ELS, respectively [l] . The organism has a high internal salt concentration [2] , and accordingly the complex is, as expected, optimally stable in high salt concentrations (greater than 3 M KCl). However, the complex is not stable in salt concentrations less than about 1 M. We shall show here that the breakdown of the complex that is observed as the salt concentration is lowered is correlated with a loss of secondary structure in the binding proteins, rather than a simple charge repulsion between the nucleic acid phosphates and carboxylates of these highly acidic proteins.
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