Characterization of mRNA-protein complexes from mammalian cells

Nucleic Acids Res. 1977 Apr;4(4):899-915. doi: 10.1093/nar/4.4.899.

Abstract

In a previous report we described the use of oligo(dT)-cellulose for the isolation of mRNA-protein complexes from EDTA-dissociated polysomes extracted from normally growing or adenovirus infected KB-cells (I). Experiments presented here provide evidence that proteins involved in these complexes bind specifically to mRNA since: a) the proteins and mRNA cosediment through sucrose gradients, b) they adsorb and elute from oligo(dT)-cellulose together, and c) analysis of the products from ribonuclease digestion experiments show that the poly (A) end and a separate small fraction of the mRNA are resistant to the enzymes and attached to protein.

MeSH terms

  • Adenoviridae*
  • Cellulose / analogs & derivatives
  • Chemical Phenomena
  • Chemistry
  • HeLa Cells
  • Nucleoproteins* / metabolism
  • Polyribosomes / analysis
  • Protein Binding
  • RNA, Messenger* / metabolism
  • Ribonucleases
  • Ribonucleoproteins* / isolation & purification
  • Ribonucleoproteins* / metabolism

Substances

  • Nucleoproteins
  • RNA, Messenger
  • Ribonucleoproteins
  • Cellulose
  • Ribonucleases