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The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins
Author(s) -
Soufi Boumediene,
Gnad Florian,
Jensen Peter Ruhdal,
Petranovic Dina,
Mann Matthias,
Mijakovic Ivan,
Macek Boris
Publication year - 2008
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800069
Subject(s) - lactococcus lactis , phosphorylation , bacillus subtilis , biology , phosphoproteomics , protein phosphorylation , biochemistry , bacteria , escherichia coli , proteomics , lactic acid , genetics , protein kinase a , gene
Recent phosphoproteomics studies of several bacterial species have firmly established protein phosphorylation on Ser/Thr/Tyr residues as a PTM in bacteria. In particular, our recent reports on the Ser/Thr/Tyr phosphoproteomes of bacterial model organisms Bacillus subtilis and Escherichia coli detected over 100 phosphorylation events in each of the bacterial species. Here we extend our analyses to Lactococcus lactis , a lactic acid bacterium widely employed by the food industry, in which protein phosphorylation at Ser/Thr/Tyr residues was barely studied at all. Despite the lack of almost any prior evidence of Ser/Thr/Tyr protein phosphorylation in L. lactis , we identified a phosphoproteome of a size comparable to that of E. coli and B. subtilis , with 73 phosphorylation sites distributed over 63 different proteins. The presence of several multiply phosphorylated proteins, as well as over‐representation of phosphothreonines seems to be the distinguishing features of the L. lactis phosphoproteome. Evolutionary comparison and the conservation of phosphorylation sites in different bacterial organisms indicate that a majority of the detected phosphorylation sites are species–specific, and therefore have probably co‐evolved with the adaptation of the bacterial species to their present‐day ecological niches.