Polynucleotide . ribosomal-protein complexes and their decoding properties

Eur J Biochem. 1982 May 17;124(2):275-81. doi: 10.1111/j.1432-1033.1982.tb06588.x.

Abstract

Polyadenylic acid, polycytidylic acid, polyuridylic acid or phage MS2 RNA, immobilized on Sepharose, form a complex with Escherichia coli ribosomal proteins. Regardless of their particular nucleotide composition, all four polynucleotides bind an invariable set of proteins consisting of S1, S3, S4, S5, S9, S13, L2 and L17. We found that these polynucleotide . protein complexes bind tRNA. Furthermore, it was possible to show that the poly(A) . protein and poly(U) . protein complexes select efficiently their cognate tRNAs, tRNALys and tRNAPhe respectively. This important functional property of the polynucleotide . protein complexes suggests that these ribosomal proteins belong in the ribosome to a functional domain responsible for the decoding of mRNA.

MeSH terms

  • Coliphages / genetics
  • Escherichia coli / genetics
  • Kinetics
  • Macromolecular Substances
  • Molecular Weight
  • Poly A / genetics
  • Poly C / genetics
  • Poly U / genetics
  • Polyribonucleotides / genetics*
  • RNA, Messenger / genetics
  • RNA, Transfer / genetics
  • RNA, Viral / genetics*
  • Ribosomal Proteins / genetics*

Substances

  • Macromolecular Substances
  • Polyribonucleotides
  • RNA, Messenger
  • RNA, Viral
  • Ribosomal Proteins
  • Poly A
  • Poly U
  • Poly C
  • RNA, Transfer