Antiterminator protein GlpP of Bacillus subtilis binds to glpD leader mRNA

被引：25

作者：

Glatz, E ^{[1
]}

Persson, M ^{[1
]}

Rutberg, B ^{[1
]}

机构：

[1] Univ Lund, Dept Microbiol, S-22362 Lund, Sweden

来源：

MICROBIOLOGY-UK | 1998年 / 144卷

关键词：

antitermination; GlpP; mRNA binding; glycerol-3-phosphate dehydrogenase; Bacillus subtilis;

D O I：

10.1099/00221287-144-2-449

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The Bacillus subtilis glpD gene encodes glycerol-3-phosphate (G3P) dehydrogenase. Expression of glpD is mainly controlled by termination/antitermination of transcription at an inverted repeat in the glpD leader. Antitermination is mediated by the antiterminator protein GlpP in the presence of G3P. In this paper, interaction between GlpP and glpD leader mRNA in vivo and in vitro is reported. In vivo, the antiterminating effect of GlpP can be titrated in a strain carrying the glpD leader on a plasmid. GlpP has been purified and gel shift experiments have shown that it binds to glpD leader mRNA in vitro. GlpP is not similar to other known antiterminator proteins, but database searches have revealed an Escherichia coli ORF which has a high degree of similarity to GlpP.

引用

页码：449 / 456

页数：8

共 33 条

[1] VECTORS BEARING A HYBRID TRP-LAC PROMOTER USEFUL FOR REGULATED EXPRESSION OF CLONED GENES IN ESCHERICHIA-COLI [J].