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Updated: Aug 12, 2026

Rapid Verification of Terminators Using the pGR-Blue Plasmid and Golden Gate Assembly
Published on: April 25, 2016
Antiterminator protein GlpP of Bacillus subtilis binds to glpD leader mRNA
Elisabeth Glatz1, Martin Persson1, Blanka Rutberg1
1Department of Microbiology, Lund University, Sölvegatan 12, S-223 62 Lund, Sweden.
Abstract:
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.
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