Stabilization of an RNA molecule by 3'-terminal poly (A)-induced inhibition of RNase activity

J Biol Chem. 1976 Jun 10;251(11):3287-93.

Abstract

The inhibitory properties of poly(A) on human spleen ribonuclease have been investigated. Hydrolytic activity has been shown to be strongly inhibited by poly(A) contained within RNAs isolated from a variety of natural sources. Furthermore, poly(A) segments of varying length have been covalently linked at the 3' terminus of Escherichia coli 5 S rRNA by polynucleotide phosphorylase in an attempt to construct an in vitro demonstration of the stabilization of RNA which contains poly(A). The extent to which these poly(A) tracts, varying from 4 to 132 nucleotides in length, could inhibit endonucleolytic attack on the 5 S rRNA to which they are linked was found to be dependent upon their length and upon small changes in spermidine concentration. The consequences of these findings are discussed in terms of a possible role for poly(A).

MeSH terms

  • Enzyme Activation / drug effects
  • Escherichia coli
  • Humans
  • Kinetics
  • Poly A / pharmacology*
  • Polyribonucleotide Nucleotidyltransferase / metabolism
  • RNA / metabolism*
  • RNA, Bacterial / metabolism*
  • RNA, Ribosomal
  • Ribonucleases / isolation & purification
  • Ribonucleases / metabolism*
  • Spermidine / pharmacology
  • Spleen / enzymology

Substances

  • RNA, Bacterial
  • RNA, Ribosomal
  • Poly A
  • RNA
  • Polyribonucleotide Nucleotidyltransferase
  • Ribonucleases
  • Spermidine