Identification by affinity chromatography of the eukaryotic ribosomal proteins that bind to 5 S ribosomal ribonucleic acid.
Rat liver 5 S ribosomal RNA was oxidized with periodate and coupled by its 3' terminus to Sepharose 4B through an adipic acid dihydrazide spacer. The ribosomal proteins that bind to that nucleic acid were isolated by affinity chromatography and identified by electrophoresis in polyacrylamide gels. The eukaryotic 5 S rRNA binding proteins were L6 and L19: small amounts of L7, L23', L27/L27', L35', and L39 also were bound to the affinity column, but whether they associate directly and specifically with 5 S rRNA is not known. The proteins of the 40 S subunit of rat liver ribosomes did not bind to the 5 S rRNA affintiy column, nor did the proteins of either the large or small subparticle of Escherichia coli ribosomes.
D000818:Animals; D002846:Chromatography, Affinity; D008099:Liver / Q000378:metabolism; D008970:Molecular Weight; D011485:Protein Binding; D012335:RNA, Ribosomal / Q000378:metabolism; D051381:Rats; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism
D012335:RNA, Ribosomal; D012269:Ribosomal Proteins