Metabolic stability of messenger ribonucleoprotein in HeLa cells.
The proteins bound to HeLa cell polyribosomal messenger RNA were isolated by subjecting salt-washed, puromycin-disassembled polyribosomes to a limited digestion with pancreatic ribonuclease (ref. 1, Auerbach, S. and Pederson, T. (1975) Biochem. Biophys. Res. Commun. 63, 149-153). Label-chase experiments with radioactive amino acids revealed that the in vivo decay kinetics of the messenger RNA-associated proteins were approximately first-order, with t1/2 equal 13-15 h. The results suggest that HeLa messenger RNA and its specific set of associated proteins do not behave as single units metabolically.
D004355:Drug Stability; D006207:Half-Life; D006367:HeLa Cells / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D009363:Neoplasm Proteins / Q000378:metabolism*; D009698:Nucleoproteins / Q000378:metabolism*; D011132:Polyribosomes / Q000378:metabolism*; D011485:Protein Binding; D012333:RNA, Messenger / Q000378:metabolism*; D012334:RNA, Neoplasm / Q000378:metabolism*; D012260:Ribonucleases; D012270:Ribosomes / Q000378:metabolism; D013997:Time Factors
D046911:Macromolecular Substances; D009363:Neoplasm Proteins; D009698:Nucleoproteins; D012333:RNA, Messenger; D012334:RNA, Neoplasm; D012260:Ribonucleases