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J. Biol. Chem., Vol. 277, Issue 1, 32-39, January 4, 2002
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From the Unité de Biochimie et Structure des Protéines,
Institut National de la Recherche Agronomique,
78352 Jouy en Josas cedex, France
The functions necessary for bacterial growth
strongly depend on the features of the bacteria and the components of
the growth media. Our objective was to identify the functions essential
to the optimum growth of Streptococcus thermophilus in
milk. Using random insertional mutagenesis on a S. thermophilus strain chosen for its ability to grow rapidly in
milk, we obtained several mutants incapable of rapid growth in milk. We
isolated and characterized one of these mutants in which an
amiA1 gene encoding an oligopeptide-binding protein (OBP)
was interrupted. This gene was a part of an operon containing all the
components of an ATP binding cassette transporter. Three highly
homologous amiA genes encoding OBPs work with the same
components of the ATP transport system. Their simultaneous inactivation
led to a drastic diminution in the growth rate in milk and the absence
of growth in chemically defined medium containing peptides as the
nitrogen source. We constructed single and multiple negative mutants
for AmiAs and cell wall proteinase (PrtS), the only proteinase capable
of hydrolyzing casein oligopeptides outside the cell. Growth
experiments in chemically defined medium containing peptides indicated
that AmiA1, AmiA2, and AmiA3 exhibited overlapping substrate
specificities, and that the whole system allows the transport of
peptides containing from 3 to 23 residues.
Three Oligopeptide-binding Proteins Are Involved in the
Oligopeptide Transport of Streptococcus
thermophilus*
*
This work was supported by Danone Vitapole Recherche,
Rhodia-Food, and Sodiaal.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
33-1-34-65-21-49; Fax: 33-1-34-65-21-63; E-mail:
monnet@jouy.inra.fr.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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