Frameshifting in the expression of the Escherichia coli trpR gene |
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Authors: | Itai Benhar Chaya Miller Hanna Engelberg-Kulka |
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Affiliation: | Department of Molecular Biology, Hebrew University, Hadassah Medical School, Jerusalem, Israel. |
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Abstract: | The trpR gene of Escherichia coli carries an open reading frame that encodes the trp repressor, 108 amino acids long. Here we show that translation of an additional (+1) reading frame of trpR occurs both in vivo and in vitro. This results in the synthesis of a stable +1 frame polypeptide. Using site-specific mutagenesis, immunological techniques and amino acid sequencing we have found that the N-terminus of the +1 frame product and that of the known 0 frame product are identical but that their C-termini differ. Our results are discussed in relation to the role of natural frameshifting as a regulatory mechanism of gene expression in general, and with respect to tryptophan biosynthesis in particular. |
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