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Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. II. Localization of the amino acid replacement in protein S17 from a neaA mutant

par Yaguchi, Makoto;Wittmann, Heinz Günter;Cabezón, Teresa ;DeWilde, Michel;Villarroel, Raimundo;Herzog, Albert ;Bollen, Alex
Référence Journal of Molecular Biology, 104, 3, page (617-620)
Publication Publié, 1976-07

Article révisé par les pairs

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Résumé :

A mutant of Escherichia coli strain K12S, neaR301, resistant to the antibiotic neamine was found to have an altered 30 S ribosomal protein S17. The modification involves a change in the electrophoretic mobility of this protein. S17 proteins wore purified from the mutant and the parental strain, respectively, and the amino acid compositions of all tryptic peptides were compared. The results show that the mutational alteration involves a replacement of histidine by proline in peptide T8 from mutant neaR301. The amino acid replacement is located at position 30 of the S17 protein chain. We conclude, therefore, that the mutation neaR301 affects the structural gene for protein S17 (rps Q). © 1976.