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Isolation and characterization of temperature-sensitive mutants of Escherichia coli with altered ribosomal proteins

✍ Scribed by Isono, Katsumi ;Krauss, Johanna ;Hirota, Yukinori

Publisher
Springer
Year
1976
Tongue
English
Weight
538 KB
Volume
149
Category
Article
ISSN
0026-8925

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✦ Synopsis

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.

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Alteration of ribosomal protein L6 in mu
Alteration of ribosomal protein L6 in mutants of Escherichia coli resistant to gentamicin
✍ Buckel, P. ;Buchberger, A. ;BΓΆck, A. ;Wittmann, H. G. πŸ“‚ Article πŸ“… 1977 πŸ› Springer 🌐 English βš– 773 KB

Spontaneous and ethylrnethane-sulfonate induced mutants of Escherichia coli resistant to gentamicin sulfate were isolated and investigated for alterations in the ribosomal protein pattern. It was found by two-dimensional polyacrylamide gel electrophoresis that three independently isolated strains di