Highly phosphorylated bacterial proteins.
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.
Rosen
Ran
R
Department of Molecular Microbiology and Biotechnology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Becher
Dörte
D
Büttner
Knut
K
Biran
Dvora
D
Hecker
Michael
M
Ron
Eliora Z
EZ
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D015153:Blotting, Western; D049109:Cell Proliferation; D030562:Databases, Protein; D015180:Electrophoresis, Gel, Two-Dimensional; D004926:Escherichia coli / Q000378:metabolism; D005838:Genotype; D006863:Hydrogen-Ion Concentration; D015151:Immunoblotting; D047468:Immunoprecipitation; D013058:Mass Spectrometry; D010766:Phosphorylation; D020543:Proteome; D040901:Proteomics; D013696:Temperature
D001426:Bacterial Proteins; D020543:Proteome