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Franziska Mika

Publications and source records attributed to Franziska Mika.

2 recordsLinked to original sources

Poly(A)-polymerase I links transcription with mRNA degradation via sigmaS proteolysis.

Bacteria rapidly adapt to changes in growth conditions through control of transcription and specific mRNA degradation. Interplay of both mechanisms must exist in order to achieve fine-tuned regulation of gene expression. Transcription of the Escherichia coli bolA gene is mediated by the RpoS/sigmaS transcription factor in response to environmental signals. In this report it is shown that the mechanisms of bolA1p mRNA transcription and degradation are tightly connected at the onset of stationary phase and in response to sudden carbon starvation. In stationary phase, bolA1p mRNA levels were reduced 2.5-fold in a poly(A)-polymerase I (PAPI) mutant, explained by the significant threefold reduction in sigmaS protein levels in the same strain. Furthermore, fusions with the rpoS gene, analysis of the stability of sigmaS and the levels of RssB indicate that the absence of PAPI enhances RssB-mediated sigmaS proteolysis specifically in starved cells. The fact that PAPI induces higher cellular levels of a global regulator is a novel finding of wide biological significance. PAPI could work as a linker between transcription and mRNA degradation with the ultimate goal of adapting and surviving to growth-limiting conditions.

Bacterial Proteins↗

A two-component phosphotransfer network involving ArcB, ArcA, and RssB coordinates synthesis and proteolysis of sigmaS (RpoS) in E. coli.

The general stress sigma factor sigma(S) (RpoS) in Escherichia coli is controlled at the levels of transcription, translation, and proteolysis. Here we demonstrate that the phosphorylated response regulator ArcA is a direct repressor of rpoS transcription that binds to two sites flanking the major rpoS promoter, with the upstream site overlapping an activating cAMP-CRP-binding site. The histidine sensor kinase ArcB not only phosphorylates ArcA, but also the sigma(S) proteolytic targeting factor RssB, and thereby stimulates sigma(S) proteolysis. Thus, ArcB/ArcA/RssB constitute a branched "three-component system", which coordinates rpoS transcription and sigma(S) proteolysis and thereby maintains low sigma(S) levels in rapidly growing cells. We suggest that the redox state of the quinones, which controls autophosphorylation of ArcB, not only monitors oxygen but also energy supply, and we show that the ArcB/ArcA/RssB system is involved in sigma(S) induction during entry into starvation conditions. Moreover, this induction is enhanced by a positive feedback that involves sigma(S)-dependent induction of ArcA, which further reduces sigma(S) proteolysis, probably by competing with RssB for residual phosphorylation by ArcB.

Bacterial Outer Membrane Proteins↗