Isolation and characterization of temperature-sensitive mutants of Escherichia coli with altered ribosomal proteins.
The ribosomal proteins of temperature-sensitive mutants of Escherichia coli isolated independently after mutagenesis with nitrosoguanidine were analyzed by two-dimensional gel electrophoresis. Out of 400 mutants analyzed, 60 mutants (15%) showed alterations in a total of 22 different ribosomal proteins. The proteins altered in these mutants are S2, S4, S6, S7, S8, S10, S15, S16, S18, L1, L3, L6, L10, L11, L14, L15, L17, L18, L19, L22, L23 and L24. 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. The importance of these mutants for structural and functional analyses of ribosomes is discussed.
D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000302:isolation & purification / Q000378:metabolism*; D009154:Mutation; D012269:Ribosomal Proteins / Q000378:metabolism*; D013045:Species Specificity; D013696:Temperature
D012269:Ribosomal Proteins