Abstract
The Escherichia coli dnaX gene encodes both the τ and γ subunits of DNA polymerase III holoenzyme in one reading frame. The 71.1 kDa τ and the shorter γ share N-terminal sequences. Mutagenesis of a potential ribosomal frameshift signal located at codons 428-430 without changing the amino acid sequence of the τ product, eliminated detectable synthesis of the γ subunit, suggesting that the reading frame is shifted at that sequence and γ is terminated by a nonsense codon located in the -1 frame 3 nucleotides downstream of the signal. This seems to be the first known case of a frameshift which is used, along with the termination codon in the -1 frame, to terminate a peptide within a reading frame. [Mutagenesis of a dibasic peptide (lys-lys) at codons 498-499, the site at which a τLacz fusion protein was cleaved in vitro (1) had no effect on γ formation in vivo, suggesting that cleavage observed in vitro is not the mechanism of γ formation in vivo.] © 1990 Oxford University Press.
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CITATION STYLE
Blinkowa, A. L., & Walker, J. R. (1990). Programmed ribosomal frameshifting generates the Escherichia coli DNA polymerase III γ subunit from within the τ subunit reading frame. Nucleic Acids Research, 18(7), 1725–1729. https://doi.org/10.1093/nar/18.7.1725
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