Open AccessThe main cold shock protein of Listeria monocytogenes belongs to the family of ferritin‐like proteins
Author(s) -
Hébraud Michel,
Guzzo Jean
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09257.x
Subject(s) - listeria monocytogenes , cold shock domain , ferritin , shock (circulatory) , microbiology and biotechnology , listeria , chemistry , biology , bacteria , biochemistry , genetics , medicine , gene , rna
The transfer of the food‐borne pathogen Listeria monocytogenes from 30 to 5°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 in flp mRNA amount after a downshift but also an upshift in temperature.