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PubMed · 15378765

Highly phosphorylated bacterial proteins.

Ran Rosen·Dörte Becher·Knut Büttner·Dvora Biran·Michael Hecker·Eliora Z Ron
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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.

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Bacterial ProteinsBlotting, WesternCell ProliferationDatabases, ProteinElectrophoresis, Gel, Two-DimensionalEscherichia coliGenotypeHydrogen-Ion ConcentrationImmunoblottingImmunoprecipitationMass SpectrometryPhosphorylationProteomeProteomicsTemperatureJournal ArticleResearch Support, Non-U.S. Gov't

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Ran Rosen, Dörte Becher, Knut Büttner, Dvora Biran, Michael Hecker, Eliora Z Ron. 2004. Highly phosphorylated bacterial proteins.. https://doi.org/10.1002/pmic.200400890

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