Non-enzymatic Translocation in Ribosomes from Streptomycin-resistant Mutants of Escherichia Coli

Overview

Journal Mol Gen Genet

Specialties Genetics
Molecular Biology

Date 1975 Jul 10

PMID 1097889

Citations 8

Authors

L S Asatryan

A S Spirin

Affiliations

Soon will be listed here.

Abstract

The capablity of ribosomes of four types of streptomycin-resistant mutants (A1, A2, A40 and A60) for non-enzymatic (EF-G--GTP-independent) translocation was tested. It was found that an A40 type mutation (amino acid replacement in position 87 of the protein S12 polypeptide chain) leads to activation of the capablity of the ribosome to perform spontaneous non-enzymatic translocation, while type A1, A2 and A60 mutations (amino acid replacements in position 42 of protein S12) does not give such an effect. Thus, it is shown that non-enzymatic translocation can be activated not only by the earlier described damage of the protein S12 by para-chloromercuribenzoate or by the complete removal of protein S12, but also by a definate mutational alteration of the protein. Preliminary data are also reported on the possibility of activating non-enzymatic translocation by combinations of mutational alterations of the ribosomal proteins other than protein S12 but interdepending with it (such as S4 and S5).

Citing Articles

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Posttranslational Modifications of Ribosomal Proteins in Escherichia coli.

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RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli.

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Multiple defects in translation associated with altered ribosomal protein L4.

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