Highly phosphorylated bacterial proteins

Proteomics
Ran RosenEliora Z Ron

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.

Citations

Jun 21, 2006·Plant Molecular Biology·Barbara Hohn, Thomas Hohn
Dec 17, 2008·Analytical Biochemistry·Kristina HempelEliora Z Ron
Sep 21, 2007·Biochimica Et Biophysica Acta·Boumediene SoufiIvan Mijakovic
Nov 11, 2006·Molecular and Cellular Endocrinology·L LabriolaM C Sogayar
Jul 5, 2011·Proteomics·Boris Macek, Ivan Mijakovic
Jul 5, 2011·Proteomics·Ran Rosen, Eliora Z Ron
May 3, 2014·Anaerobe·Anne-Cécile Hochart-BehraJosette Behra-Miellet
Jan 16, 2007·Molecular & Cellular Proteomics : MCP·Boris MacekMatthias Mann
Mar 15, 2020·Microbiological Research·Elodie DussertJosette Behra-Miellet

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