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The Gram-positive model bacterium  Bacillus subtilis  contains two glutamate dehydro genase-encoding genes,  rocG  and  gudB . While the  rocG  gene encodes the functional GDH, the  gudB  gene is cryptic ( gudB CR  ) in the laboratory strain 168 due to a perfect 18 bp-long direct repeat that renders the GudB enzyme inactive and unstable. Although constitutively expressed the GudB CR  protein can hardly be detected in  B. subtilis  as it is rapidly degraded within stationary growth phase. Its high instability qualifies GudB CR  as a model substrate for studying protein turnover in  B. subtilis . Recently, we have developed a visual screen to monitor the GudB CR  stability in the cell using a GFP-GudB CR  fusion. Using fluorescent microscopy we found that the GFP protein is simultaneously degraded together with GudB CR . This allows us to analyze the stability of GudB CR  in living cells. By combining the visual screen with a transposon mutagenesis approach we looked for mutants that show an increased fluorescence signal compared to the wild type indicating a stabilized GFP-GudB CR  fusion. We observed, that disruption of the arginine kinase encoding gene  mcsB  upon transposon insertion leads to increased amounts of the GFP-GudB CR  fusion in this mutant. Deletion of the cognate arginine phosphatase YwlE in contrast results in reduced levels of the GFP-GudB CR  fusion. Recently, it was shown that the kinase McsB is involved in phosphorylation of GudB CR  on arginine residues. Here we show that selected arginine-lysine point mutations of GudB CR  exhibit no influence on degradation. The activity of McsB and YwlE, however, are crucial for the activation and inhibition, respectively, of a proteolytic machinery that efficiently degrades the unstable GudB CR  protein in  B. subtilis .

Factors that mediate and prevent degradation of the inactive and unstable GudB protein in Bacillus subtilis