Abstract
Streptococcus thermophilus PB18 can grow between 20° and 52°C and is resistant to various stresses such as heat, acidic or cold shock. During cold shock, a protein of 21.5 kDa was previously shown to be induced in S. thermophilus. In addition to its cold-shock induction, 2D-PAGE revealed that the 21.5-kDa protein was also expressed during the stationary phase of growth. The recent access to the genome sequence of S. thermophilus LMG18311 allowed the identification of a 173-amino acid protein displaying a strong homology between the 21.5-kDa protein and members of the Dps family of proteins. Specific staining of non-denaturing polyacrylamide gel electrophoresis (ND-PAGE) followed by two-dimensional PAGE (2D-PAGE) showed that the 21.5-kDa protein was an iron-binding protein.
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Nicodème, ., Perrin, ., Hols, . et al. Identification of an Iron-Binding Protein of the Dps Family Expressed by Streptococcus thermophilus . Curr Microbiol 48, 51–56 (2004). https://doi.org/10.1007/s00284-003-4116-3
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DOI: https://doi.org/10.1007/s00284-003-4116-3