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Application of an In vitro DNA Protection Assay to Visualize Stress Mediation Properties of the Dps Protein
Published on: May 31, 2013
Identification of an iron-binding protein of the Dps family expressed by Streptococcus thermophilus
Muriel Nicodème1, Clarisse Perrin, Pascal Hols
1Laboratoire des BioSciences de l'Aliment , U.C. INRA n(o)885, Faculté des Sciences et Techniques, Université Henri Poincaré-Nancy 1, B.P. 239, 54506 Vandoeuvre-lès-Nancy Cedex, France.
Abstract:
Streptococcus thermophilus PB18 can grow between 20 degrees and 52 degrees 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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