FRAMESHIFTING IN THE EXPRESSION OF THE ESCHERICHIA-COLI TRPR GENE

被引：23

作者：

BENHAR, I ^{[1
]}

MILLER, C ^{[1
]}

ENGELBERGKULKA, H ^{[1
]}

机构：

[1] HEBREW UNIV JERUSALEM,HADASSAH MED SCH,DEPT MOLEC BIOL,IL-91010 JERUSALEM,ISRAEL

来源：

MOLECULAR MICROBIOLOGY | 1992年 / 6卷 / 19期

关键词：

D O I：

10.1111/j.1365-2958.1992.tb01457.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2777 / 2784

页数：8

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