Benhar I, Miller C, Engelberg-Kulka H
Department of Molecular Biology, Hebrew University, Hadassah Medical School, Jerusalem, Israel.
Mol Microbiol. 1992 Oct;6(19):2777-84. doi: 10.1111/j.1365-2958.1992.tb01457.x.
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.
大肠杆菌的trpR基因带有一个开放阅读框，其编码的trp阻遏蛋白由108个氨基酸组成。我们在此表明，trpR额外的（+1）阅读框在体内和体外均会发生翻译。这导致了一种稳定的+1框多肽的合成。通过位点特异性诱变、免疫学技术和氨基酸测序，我们发现+1框产物的N端与已知的0框产物的N端相同，但它们的C端不同。我们结合自然移码作为一般基因表达调控机制的作用，特别是关于色氨酸生物合成来讨论我们的结果。
