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FEMS Microbiol Lett. 2000 Sep 1;190(1):29-34.

The main cold shock protein of Listeria monocytogenes belongs to the family of ferritin-like proteins.

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Unité de Recherches sur la Viande, Institut National de la Recherche Agronomique de Theix, Champanelle, France.


The transfer of the food-borne pathogen Listeria monocytogenes from 30 to 5 degrees C was characterized by the sharp induction of a low molecular mass protein. This major cold shock protein has an isoelectric point at pH 5.1 and a molecular mass of about 18 kDa, as observed on two-dimensional gel electrophoresis (2-DE) pattern. Its N-terminal sequence, obtained from the 2-DE spot, shared a complete sequence identity with a Listeria innocua non-heme iron-binding ferritin. The purification of these ferritin-like proteins (Flp) revealed a native molecular mass of about 100-110 kDa which indicates a polypeptide composed of six 18 kDa-subunits. Northern analysis indicated the presence of a 0.8-kb monocistronic mRNA in exponential growing cells and an important increase inflp mRNA amount after a downshift but also an upshift in temperature.

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