Katsumi Isono

TL;DR: An improved method for the two-dimensional electrophoretic analysis of ribosomal proteins on acrylamide gel slabs has been developed by combining the procedures for the first dimension of Mets and Bogorad (1974) and for the second dimension of Kaltschmidt and Wittmann (1970) and by introducing several modification.

TL;DR: A thermosensitive mutant (JE386) of Escherichia coli which harbours an alteration in protein S5 of the smaller ribosomal subunit has been isolated and it has been found that the wild-type allele is dominant over the mutant one.

TL;DR: A large number of them (25 mutants) have mutations in protein S4 of the small subunit, while four mutants showed alterations in protein L6 of the large subunit that are important for structural and functional analyses of ribosomes.

TL;DR: It was found that the acetylase activity specific for protein L12 was negligible, when assayed in vitro, in the high-speed supernatant prepared from mutant cells, indicating that the three mutants contain mutations in the gene rimL that codes for an acetylating enzyme specific for ribosomal protein L 12.

TL;DR: Temperature-sensitive mutants of an Escherichia coli K-12 strain PA3092 have been isolated following mutagenesis with nitrosoguanidine and their ribosomal proteins analyzed by two-dimensional gel electrophoresis and a mutant has been obtained which apparently lacks the protein S20 (L26) with a concomitant reduction to a great extent of the polypeptide synthetic activity of the small subunit.