Identification of an Iron-Binding Protein of the Dps Family Expressed by Streptococcus thermophilus
- 2004-01-01
- Current Microbiology 48(1)
- M. Nicodème
- C. Perrin
- P. Hols
- P. Bracquart
- J. Gaillard
- PubMed: 15018103
- DOI: 10.1007/s00284-003-4116-3
Study Design
- Methods
- n/a
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.