Protein synthesis and aging: studies with cell-free mammalian systems

Fed Proc. 1979 May;38(6):1979-83.

Abstract

A cell-free system devoid of polysomes, which translates natural mRNA, has been prepared from rat liver. It contains ribosomal subunits, ribosomes, aminoacyl-tRNA synthetases, tRNAs, and protein factors necessary for translation. Protein synthesis required an energy-generating system, mRNA, and 3 mM Mg2+ concentration, and it was inhibited by 7-methylguanylic acid. The total extent and the rate of protein synthesis were approximately 30% greater when the translating system was prepared from livers of 3-month-old rats, as compared to 30-month-old rats. A ribosome-free fraction containing the protein factors required for translation was also prepared from 3-month-old and 30-month-old rat livers and brains, by extraction with 0.5 M KCl. The high-salt extracts were analyzed for elongation factors EF-1 and EF-2 in a poly(U) translating system. Although the activity of EF-2 was similar in preparations from young and old rats, the EF-1 activity in the 3-month-old rat livers and brains was 30 to 40% greater than in 30-month-old animals. The protein synthesizing activity of high salt-washed ribosomes stripped of endogenous peptidyl-tRNA and mRNA, from livers and brains of young and old animals, was the same.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aging*
  • Amino Acyl-tRNA Synthetases / metabolism
  • Animals
  • Brain / ultrastructure
  • Liver / ultrastructure
  • Peptide Chain Elongation, Translational
  • Peptide Chain Initiation, Translational
  • Peptide Elongation Factors / metabolism
  • Peptide Initiation Factors / metabolism
  • Protein Biosynthesis*
  • RNA, Messenger / metabolism
  • RNA, Transfer / metabolism
  • Rats
  • Ribonucleoproteins / biosynthesis
  • Ribosomes / metabolism

Substances

  • Peptide Elongation Factors
  • Peptide Initiation Factors
  • RNA, Messenger
  • Ribonucleoproteins
  • RNA, Transfer
  • Amino Acyl-tRNA Synthetases