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. 1969 Jul;99(1):91–100. doi: 10.1128/jb.99.1.91-100.1969

Fidelity of Initiation of Protein Synthesis After Premature Chain Termination in Polarity Mutants1

S J Parsons a,2, R O Burns a
PMCID: PMC249971  PMID: 4979448

Abstract

β-Isopropylmalate dehydrogenase, the product of the second cistron of the leucine operon in Salmonella typhimurium, produced by strains bearing nonsense or frameshift mutations in the first cistron of the operon was shown to be homogeneous as judged by electrophoretic and immunological techniques. Amino terminal analyses suggest that the enzyme produced by the mutant strains is identical with the wild-type enzyme. This view is supported by the observation that a nonsense mutant strain β-isopropylmalate dehydrogenase copurifies with the wild-type enzyme. The results suggest that the uncoupling of normal chain termination and reinitiation does not interfere with the fidelity of subsequent polypeptide chain initiation in a polycistronic messenger ribonucleic acid.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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