Open AccessA proteomic analysis of the salt stress response of Listeria monocytogenes
Author(s) -
Duché Ophélie,
Trémoulet Frédéric,
Namane Abdelkader,
Labadie Jean
Publication year - 2002
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.1574-6968.2002.tb11389.x
Subject(s) - listeria monocytogenes , ribosomal protein , gel electrophoresis , bacteria , listeria , chemistry , osmotic shock , proteome , biochemistry , salt (chemistry) , proteomics , microbiology and biotechnology , biology , food science , ribosome , genetics , gene , rna
Protein variations in Listeria monocytogenes were analyzed by 2‐D electrophoresis. Bacteria were grown either in a rich medium or in a chemically defined medium. Three proteins, which are more expressed in the chemically defined medium than in the rich medium, were identified by mass spectrometry. They are closely related to AppA, Ctc and YvyD. After an osmotic shock, according to the medium and the NaCl concentration, the synthesis rate ( P <0.05) of 59 proteins is altered by salinity. Half of them were more expressed, some of these proteins were closely related to Ctc, GbuA and the 30S ribosomal protein S6. Among the proteins which were down‐expressed in the presence of salt, two were similar to AckA and PdhD.