Synthesis and turnover of ribosomal proteins in the absence of 60S subunit assembly in Saccharomyces cerevisiae

Mol Gen Genet. 1977 Dec 9;157(3):327-32. doi: 10.1007/BF00268670.


We have measured the synthesis and stability of ribosomal proteins in a temperature sensitive strain of yeast which at the restrictive temperature is specifically blocked in the processing of 27S ribosomal precursor RNA. We find that in the absence of 60S ribosomal subunit assembly, the synthesis of all the ribosomal proteins studied continued. However, the proteins of the 60S subunit fail to accumulate and are rapidly degraded.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Electrophoresis, Polyacrylamide Gel
  • Mutation
  • Protein Precursors / metabolism
  • RNA, Ribosomal / metabolism
  • Ribosomal Proteins / metabolism*
  • Saccharomyces cerevisiae / metabolism


  • Protein Precursors
  • RNA, Ribosomal
  • Ribosomal Proteins