30S ribosomal proteins cross-linked to 16S RNA by periodate oxidation followed by borohydride reduction.
Gel electrophoretic techniques have been used to reexamine the RNA-protein cross-linking reaction induced by periodate oxidation and borohydride reduction of 30S ribosomal subunits. The results show that a number of 30S ribosomal proteins become attached to intact 16S RNA by this method, in addition to those already published. It follows that this cross-linking technique as it stands is of little value as a topographical probe of the environment of the 3'-terminus of the 16S RNA.
D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites; D001894:Borohydrides; D004926:Escherichia coli / Q000648:ultrastructure; D010084:Oxidation-Reduction; D010504:Periodic Acid; D011485:Protein Binding; D012329:RNA, Bacterial / Q000378:metabolism; D012335:RNA, Ribosomal / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000648:ultrastructure*
D001426:Bacterial Proteins; D001894:Borohydrides; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D010504:Periodic Acid