The binding of transfer ribonucleic acids to 5 S and 5.8 S eukaryotic ribosomal ribonucleic acid-protein complexes

• Published in: The Journal of biological chemistry 1982-03, Vol.257 (5), p.2522-2527
• Main Authors: Chan, Y L, Ulbrich, N, Ackerman, E J, Todokoro, K, Slobin, L I, Safer, B, Sigler, P B, Wool, I G
• Format: Article
• Language: English
• Subjects: Animals; Liver - metabolism; Nucleoproteins - metabolism; Peptide Chain Elongation, Translational; Peptide Elongation Factor 1; Peptide Elongation Factors - metabolism; Rats; Reticulocytes; Ribonucleoproteins - metabolism; RNA, Ribosomal - metabolism; RNA, Transfer - metabolism; Saccharomyces cerevisiae
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)34955-X

Rat liver 5 S and 5.8 S rRNAs were oxidized with periodate and the 3' termini were coupled to Sepharose 4B through an adipic acid dihydrazide spacer. Ribosomal proteins were passed through the nucleic acid affinity columns to form ribonucleoprotein complexes containing the nucleic acid and the proteins that bind to it (5 S . L6, L7, L19; and 5.8 S . L6, L19, S9, S13). Pure isoaccepting species of yeast initiator-tRNA (tRNAfMet) and elongator-tRNAs (tRNAmMet, and tRNAPhe) were chromatographed on the ribosomal ribonucleoprotein affinity columns. The three rRNAs were bound to the 5 S and 5.8 S ribosomal ribonucleoprotein complexes. The elongation and initiation ternary complexes, EF-1 alpha . GTP . Phe-tRNAPhe, and eIF-2 . GTP . Met-tRNAfMet, also were bound to both ribosomal ribonucleoprotein affinity columns, whereas the binary complex EF-1 alpha . GTP and puromycin were not.