Ion effects on protein-nucleic acid interactions: the disassembly of the 50-S ribosomal subunit from the halophilic bacterium, Halobacterium cutirubrum.
The 50-S ribosomal subunits from the extreme halophilic bacterium, Halo-bacterium cutirubrum, stable structurally and functionally in concentrated salt solutions were subjected to ionic environments depleted in either K+ or Mg2+ or both. Under these conditions specific classes of proteins are released from the subunit along with the 5 S RNA. Two-dimensional electrophoretic analysis of the resultant split protein fractions indicate some mutually exclusive effects of specific ions on the binding of specific proteins to the 23 S RNA as well as on the retention of 5 S RNA within the ribosomal macrostructure.
D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D006217:Halobacterium / Q000378:metabolism*; D008274:Magnesium / Q000494:pharmacology; D009994:Osmolar Concentration; D011188:Potassium / Q000494:pharmacology; D011485:Protein Binding; D012329:RNA, Bacterial / Q000302:isolation & purification / Q000378:metabolism*; D012335:RNA, Ribosomal / Q000302:isolation & purification / Q000378:metabolism*; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D008274:Magnesium; D011188:Potassium