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Amino acid replacement in the protein S5 from a spectinomycin resistant mutant of Bacillus subtilis

✍ Scribed by Itoh, T.

Publisher
Springer
Year
1976
Tongue
English
Weight
288 KB
Volume
144
Category
Article
ISSN
0026-8925

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✦ Synopsis

Ribosomal protein S5 was isolated from wild type Bacillus subtilis ATCC 6633 and from a spectinomycin resistant mutant (BSPC 111) derived from spectinomycin sensitive to resistance is accomtrypsin and all the tryptic peptides were isolated by column- and paper-chromatography. By comparative amino acid analyses of the peptides, it was demonstrated that the S5 from the mutant differs from the wild type S5 by a replacement of one amino acid, namely lysine by isoleucine in the peptide T9. The results are compared with E. coli spectinomycin resistant mutants.

πŸ“œ SIMILAR VOLUMES

Genetic position and amino acid replacem
Genetic position and amino acid replacements of several mutations in ribosomal protein S5 from Escherichia coli
✍ Piepersberg, W. ;BΓΆck, A. ;Yaguchi, M. ;Wittmann, H. G. πŸ“‚ Article πŸ“… 1975 πŸ› Springer 🌐 English βš– 827 KB

The relative genetic position of the following four mutations of ribosomal protein S5 has been determined: spc-13, a mutation to spectinomycin resistance; stri N421 and strid1023, mutations suppressing dependence on streptomycin and sup0-1, a mutation suppressing partially the temperature-sensitive