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Journal of Bacteriology, May 1999, p. 3277-3280, Vol. 181, No. 10
Laboratoire de Génétique
Moléculaire et Cellulaire, Centre National de la Recherche
Scientifique ERS 567, Institut National de la Recherche
Agronomique, F-78850 Thiverval-Grignon, France
Received 5 November 1998/Accepted 23 February 1999
The deduced product of the Bacillus subtilis ytvP gene
is similar to that of ORF13, a gene of unknown function in
the Lactococcus lactis histidine biosynthesis operon. A
B. subtilis ytvP mutant was auxotrophic for histidine. The
only enzyme of the histidine biosynthesis pathway that remained
uncharacterized in B. subtilis was histidinol
phosphate phosphatase (HolPase), catalyzing the penultimate step of
this pathway. HolPase activity could not
be detected in crude extracts of the ytvP mutant, while
purified glutathione S-transferase-YtvP fusion
protein exhibited strong HolPase activity. These observations
demonstrated that HolPase is encoded by ytvP in
B. subtilis and led us to rename this gene hisJ. Together with the HolPase of Saccharomyces
cerevisiae and the presumed HolPases of
L. lactis and Schizosaccharomyces pombe, HisJ
constitutes a family of related enzymes that are not homologous to the
HolPases of Escherichia coli, Salmonella
typhimurium, and Haemophilus influenzae.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Histidinol Phosphate Phosphatase, Catalyzing the Penultimate Step
of the Histidine Biosynthesis Pathway, Is Encoded by
ytvP (hisJ) in Bacillus
subtilis
*
Corresponding author. Mailing address: Laboratoire de
GénétiqueMoléculaire et Cellulaire, Centre National
de la Recherche Scientifique ERS 567, Institut National de la Recherche
Agronomique, F-78850 Thiverval-Grignon, France. Phone: (33)
1.30.81.54.45. Fax: (33) 1.30.81.54.57. E-mail:
lecoq{at}platon.grignon.inra.fr.
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