TY - JOUR
T1 - Frameshifting in the expression of the Escherichia coli trpR gene
AU - Benhar, Itai
AU - Miller, Chaya
AU - Engelberg‐Kulka, Hanna
PY - 1992/10
Y1 - 1992/10
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0026674888&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2958.1992.tb01457.x
DO - 10.1111/j.1365-2958.1992.tb01457.x
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AN - SCOPUS:0026674888
SN - 0950-382X
VL - 6
SP - 2777
EP - 2784
JO - Molecular Microbiology
JF - Molecular Microbiology
IS - 19
ER -