
Effects of ribosomal mutations on the read-through of a chain termination signal: studies on the synthesis of bacteriophage lambda O gene protein in vitro.
Author(s) -
John L. Yates,
William R. Gette,
Mark E. Furth,
Masayasu Nomura
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.2.689
Subject(s) - ribosome , protein biosynthesis , ribosomal protein , biology , bacteriophage , mutant , ribosomal rna , gene , microbiology and biotechnology , dna , mutation , rna , genetics , escherichia coli
In a DNA-dependent protein-synthesizing system that contains streptomycin-sensitive ribosomes, lambda DNA directs the synthesis of two proteins that are products of the O gene. The larger is produced as a result of read-through of a UGA termination codon. In the system containing streptomycin-resistant ribosomes this read-through protein is not synthesized, indicating that the mutational alteration in the ribosomal protein S12 restricts the read-through. The mutant ribosomes also fail to synthesize the read-through coat protein of RNA phage Qbeta. In addition, the mutant ribosomes restrict suppression of amber mutations in vitro, similar to their effect in vivo.