Characterization of mRNA-protein complexes from mammalian cells.
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.
D000256:Adenoviridae; D002482:Cellulose / Q000031:analogs & derivatives; D055598:Chemical Phenomena; D002621:Chemistry; D006367:HeLa Cells; D009698:Nucleoproteins / Q000378:metabolism; D011132:Polyribosomes / Q000032:analysis; D011485:Protein Binding; D012333:RNA, Messenger / Q000378:metabolism; D012260:Ribonucleases; D012261:Ribonucleoproteins / Q000302:isolation & purification / Q000378:metabolism
D009698:Nucleoproteins; D012333:RNA, Messenger; D012261:Ribonucleoproteins; D002482:Cellulose; D012260:Ribonucleases