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Applied and Environmental Microbiology, October 2006, p. 6623-6631, Vol. 72, No. 10
0099-2240/06/$08.00+0 doi:10.1128/AEM.00624-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Eleonore Botton,
Iharilalao Dubail, and
Alain Charbit*
INSERM U-570, CHU Necker-Enfants Malades, 156, rue de Vaugirard, 75730 Paris Cedex 15, France
Received 17 March 2006/ Accepted 21 July 2006
Molecular chaperones play an essential role in the folding of nascent chain polypeptides, as well as in the refolding and degradation of misfolded or aggregated proteins. They also assist in protein translocation and participate in stress functions. We identified a gene, designated tig, encoding a protein homologous to trigger factor (TF), a cytosolic ribosome-associated chaperone, in the genome of Listeria monocytogenes. We constructed a chromosomal
tig deletion and evaluated the impact of the mutation on bacterial growth in broth under various stress conditions and on pathogenesis. The
tig deletion did not affect cell viability but impaired survival in the presence of heat and ethanol stresses. We also identified the ffh gene, encoding a protein homologous to the SRP54 eukaryotic component of the signal recognition particle. However, a
ffh deletion was not tolerated, suggesting that Ffh is essential, as it is in Bacillus subtilis and Escherichia coli. Thus, although dispensable for growth, TF is involved in the stress response of L. monocytogenes. The
tig mutant showed no or very modest intracellular survival defects in eukaryotic cells. However, in vivo it showed a reduced capacity to persist in the spleens and livers of infected mice, revealing that TF has a role in the pathogenicity of L. monocytogenes.
A.B. and E.B. contributed equally to this work.
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