The Bacillus subtilis glpD gene encodes glycerol-3-phosphate (G3P) deh
ydrogenase. Expression of glpD is mainly controlled by termination/ant
itermination of transcription at an inverted repeat in the glpD leader
. Antitermination is mediated by the antiterminator protein GlpP in th
e presence of G3P. In this paper, interaction between GlpP and glpD le
ader mRNA in vivo and in vitro is reported. In vivo, the antiterminati
ng 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 s
hown that it binds to glpD leader mRNA in vitro. GlpP is not similar t
o other known antiterminator proteins, but database searches have reve
aled an Escherichia coli ORF which has a high degree of similarity to
GlpP.