Nicodeme, M
Perrin, C.
Hols, Pascal
[UCL]
Bracquart, P
Gaillard, JL
Streptococcus thermophilus PB18 can grow between 20degrees and 52degreesC 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.
Bibliographic reference |
Nicodeme, M ; Perrin, C. ; Hols, Pascal ; Bracquart, P ; Gaillard, JL. Identification of an iron-binding protein of the Dps family expressed by Streptococcus thermophilus. In: Current Microbiology, Vol. 48, no. 1, p. 51-56 (2004) |
Permanent URL |
http://hdl.handle.net/2078.1/40448 |