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Highly phosphorylated bacterial proteins
Author(s) -
Rosen Ran,
Becher Dörte,
Büttner Knut,
Biran Dvora,
Hecker Michael,
Ron Eliora Z.
Publication year - 2004
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.200400890
Subject(s) - proteolysis , phosphorylation , biochemistry , escherichia coli , ribosomal protein , biology , protein phosphorylation , bacteria , enzyme , chemistry , microbiology and biotechnology , ribosome , protein kinase a , rna , genetics , gene
Abstract We show in Gram‐negative and Gram‐positive bacteria the appearance of highly acidic proteins, which are highly phosphorylated. This group of proteins includes many cellular proteins, such as chaperones, biosynthetic, and metabolic enzymes. These proteins accumulate under stress conditions or under conditions, which overload the proteolytic system. Pulse chase experiments using radioactive phosphate indicate that the phosphorylated proteins have a short half‐life, suggesting that they could be degradation intermediates. Moreover, results from in vitro experiments in Escherichia coli indicated that ribosomal proteins become susceptible to proteolysis after polyphosphorylation. Therefore, it is possible that the highly phosphorylated proteins represent a group of proteins tagged for degradation by phosphorylation. Such a tagging process may be involved in a general bacterial degradation pathway.