Role of the response regulator RssB in σS recognition and initiation of σS proteolysis in Escherichia coli

Klauck, Eberhard; Lingnau, Maren; Hengge‐Aronis, Regine

doi:10.1046/j.1365-2958.2001.02482.x

Cited by 67 publications

(82 citation statements)

References 47 publications

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“…It nevertheless displays residual activity that supports S degradation at a reduced rate ( Fig. 4D; Klauck et al 2001). In the strains used in Figure 4A and B, these rssB alleles were plasmid expressed under the control of the araBAD promoter (in a rssBϻTn10 genetic background; in the absence of inducer, basal RssB expression from these constructs produces cellular RssB levels comparable to those in wild-type strains [Klauck et al 2001]).…”

Section: The Histidine Sensor Kinase Arcb Stimulates S Proteolysis Bymentioning

confidence: 97%

“…Using the direct radioactive transphosphorylation assay as well as the functional RssB-S interaction assay, we found that this was not the case (data not shown). This indicates that ArcB-dependent phosphorylation of RssB is a one-way reaction and that RssB is dephosphorylated by other factors, perhaps as part of its proteolytic targeting cycle (Klauck et al 2001). This is in contrast to ArcA, for which ArcB can act as a phosphatase (Georgellis et al 1998).…”

Section: Arcb Phosphorylates and Thereby Activates The S Proteolysismentioning

confidence: 99%

“…4D; Klauck et al 2001). In the strains used in Figure 4A and B, these rssB alleles were plasmid expressed under the control of the araBAD promoter (in a rssBϻTn10 genetic background; in the absence of inducer, basal RssB expression from these constructs produces cellular RssB levels comparable to those in wild-type strains [Klauck et al 2001]). In the presence of wild-type RssB, the arcB mutation reduced the in vivo rate of S degradation from a half-life of ∼3.2 min to 6.5 min (Fig.…”

Section: The Histidine Sensor Kinase Arcb Stimulates S Proteolysis Bymentioning

confidence: 99%

“…As phosphorylated RssB does not exhibit intrinsic autophosphatase actvity and is stable over at least 2 h (Klauck et al 2001), we could also test whether ArcB can act as a phosphatase for prephosphorylated RssB and whether reverse phosphate flow from prephosphorylated RssB via ArcB 78-778 to ArcA can occur. Using the direct radioactive transphosphorylation assay as well as the functional RssB-S interaction assay, we found that this was not the case (data not shown).…”

Section: Arcb Phosphorylates and Thereby Activates The S Proteolysismentioning

confidence: 99%

“…S degradation requires the complex ATP-dependent ClpXP protease as well as the response regulator RssB, which, in its phosphorylated form, binds to S (thereby exposing a ClpX-binding site in S ), delivers S to ClpXP, and is released from the complex (Becker et al 1999;Klauck et al 2001;Zhou et al 2001). Thus, RssB acts as a proteolytic recognition or targeting factor for S .…”

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

Mika¹,

Hengge²

2005

Genes Dev.

170

150

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The general stress factor 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 S proteolytic targeting factor RssB, and thereby stimulates S proteolysis. Thus, ArcB/ArcA/RssB constitute a branched "three-component system", which coordinates rpoS transcription and S proteolysis and thereby maintains low 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 S induction during entry into starvation conditions. Moreover, this induction is enhanced by a positive feedback that involves S -dependent induction of ArcA, which further reduces S proteolysis, probably by competing with RssB for residual phosphorylation by ArcB. [Keywords: Histidine sensor kinase; response regulator; RNA polymerase; RpoS; starvation; stress] Controlled proteolysis of key regulatory factors in response to cellular and environmental signals plays a crucial role both in eukaryotic and prokaryotic cells. One of the most prominent prokaryotic examples is the degradation of the S (RpoS) subunit of RNA polymerase (RNAP) in rapidly growing Escherichia coli cells, which is inhibited in response to several stress conditions: e.g., starvation, hyperosmotic shift, or pH downshift (for a summary of S regulation, see Hengge-Aronis 2002). This results in a rapid increase of the cellular concentration of S , which competes with the vegetative subunit 70 , and thereby induces the general stress response (Hengge-Aronis 2000), which affects the expression of ∼10% of the E. coli genes (Weber et al. 2005). In parallel, rpoS transcription can be enhanced in response to poor nutritional conditions and reduced growth rates (Hengge-Aronis 2002). In addition, the efficiency of rpoS mRNA translation is controlled by various stress-sensing mechanisms that involve small regulatory RNAs and the Hfq protein (Repoila et al. 2003). Whether these levels of control operate independently and additively or are somehow coordinated, is still an open question.The present study started from the question of how S proteolysis is regulated. S degradation requires the complex ATP-dependent ClpXP protease as well as the response regulator RssB, which, in its phosphorylated form, binds to S (thereby exposing a ClpX-binding site in S ), delivers S to ClpXP, and is released from the complex (Becker et al. 1999;Klauck et al. 2001;Zhou et al. 2001). Thus, RssB acts as a proteolytic recognition or targeting factor for S . This process is regulated by various mechanisms that affect specific substrate, i.e., S recognition, and can integrate different ...

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Section: The Histidine Sensor Kinase Arcb Stimulates S Proteolysis Bymentioning

confidence: 97%

Section: Arcb Phosphorylates and Thereby Activates The S Proteolysismentioning

confidence: 99%

Section: The Histidine Sensor Kinase Arcb Stimulates S Proteolysis Bymentioning

confidence: 99%

Section: Arcb Phosphorylates and Thereby Activates The S Proteolysismentioning

confidence: 99%

mentioning

confidence: 99%

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

Mika¹,

Hengge²

2005

Genes Dev.

170

150

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Kinetics, Microbial Growth

Panikov

2010

Encyclopedia of Industrial Biotechnology

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The article summarizes basic principles, methods, and the most essential results of kinetic studies in microbiology. Microbial kinetics is based on experimental studies of all dynamic manifestations of microbial life (growth, survival, death, product formation, mutations, cell cycles, environmental effects) and analysis of underlying mechanisms using mathematical models. The article starts from introduction to basic principles of growth stoichiometry (quantitative relationships between substrates and products of microbial processes) and enzyme kinetics and then, step‐by‐step surveys simple and structured models of microbial growth, cell cycle, mutation, and population dynamics. Special emphasis is given to similarity and difference in kinetic terms as applied to chemical reactions, enzyme‐catalyzed processes, and microbial growth. The last part of the chapter is devoted to characterization of diversity of cultivation methods including various continuous methods (chemostat, turbidostat, pH‐auxostat, viscostat, bistat), batch, fed‐batch, phased and dialysis culture, plug‐flow, columns packed, colonies and biofilms.

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Double‐Strand‐Break Repair, Mutagenesis, and Stress

Rogers

Correa

Barreto

et al. 2016

Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria

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Role of the response regulator RssB in σ^S recognition and initiation of σ^S proteolysis in Escherichia coli

Abstract: SummaryIn growing Escherichia coli cells, the master regulator of the general stress response, s S (RpoS), is subject to rapid proteolysis.

Cited by 67 publications

References 47 publications

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

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

Kinetics, Microbial Growth

Double‐Strand‐Break Repair, Mutagenesis, and Stress

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Role of the response regulator RssB in σS recognition and initiation of σS proteolysis in Escherichia coli

Abstract: SummaryIn growing Escherichia coli cells, the master regulator of the general stress response, s S (RpoS), is subject to rapid proteolysis.

Cited by 67 publications

References 47 publications

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

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

Kinetics, Microbial Growth

Double‐Strand‐Break Repair, Mutagenesis, and Stress

Contact Info

Product

Resources

About

Role of the response regulator RssB in σ^S recognition and initiation of σ^S proteolysis in Escherichia coli

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

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