Crystal Structure of the Escherichia coli Regulator of σ70, Rsd, in Complex with σ70 Domain 4

Patikoglou, Georgia A.; Westblade, Lars F.; Campbell, Elizabeth A.; Lamour, Valérie; Lane, William J.; Darst, Seth A.

doi:10.1016/j.jmb.2007.06.081

Cited by 57 publications

(69 citation statements)

References 47 publications

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“…Consequently, molecular details must be deduced from biochemical analyses and from the predictions of the available structures of thermophilic RNAPs (2,3) or the C-terminal portion of E. coli 70 with AsiA (14) or the host anti-sigma factor Rsd (44). It is particularly important to test whether the H5/␤-flap tip contacts seen in the thermophilic RNAP structures apply to E. coli RNAP because the sequence of H5 deviates between these bacteria (Fig.…”

Section: Discussionmentioning

confidence: 99%

Bacteriophage T4 MotA Activator and the β-Flap Tip of RNA Polymerase Target the Same Set of σ70 Carboxyl-terminal Residues

Bonocora

Decker

Glass

et al. 2011

Journal of Biological Chemistry

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Background: Transcriptional activators interact with RNA polymerase to redefine gene expression. Results: A phage activator engages a region of the specificity factor of E. coli RNA polymerase, which is normally bound by another portion of RNA polymerase. Conclusion: Using an activator/co-activator system, the phage hijacks the host RNA polymerase. Significance: Small transcriptional factors acting on defined local regions of RNA polymerase can fundamentally change gene expression.

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Section: Discussionmentioning

confidence: 99%

Bacteriophage T4 MotA Activator and the β-Flap Tip of RNA Polymerase Target the Same Set of σ70 Carboxyl-terminal Residues

Bonocora

Decker

Glass

et al. 2011

Journal of Biological Chemistry

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“…Structural studies of the σ 70 4 /Rsd complex reveal that Rsd binds to residues of σ 70 4 that are important for both RNAP and -35 element recognition. Unlike AsiA, however, this binding does not alter the structural core of σ 70 4 ( Figure 1c; [30]). …”

Section: Regulation Of Escherichia Coli σ 70 By σ 70 -Binding Proteinsmentioning

confidence: 93%

Regulation of bacterial RNA polymerase σ factor activity: a structural perspective

Campbell

Westblade

Darst

2008

Current Opinion in Microbiology

126

119

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SummaryIn bacteria, σ factors are essential for the promoter DNA-binding specificity of RNA polymerase. The σ factors themselves are regulated by anti-σ factors that bind and inhibit their cognate σ factor, and 'appropriators' that deploy a particular σ-associated RNA polymerase to a specific promoter class. Adding to the complexity is the regulation of anti-σ factors by both anti-anti-σ factors, which turn on σ factor activity, and co-anti-σ factors that act in concert with their partner anti-σ factor to inhibit or redirect σ activity. While σ factor structure and function is highly conserved, recent results highlight the diversity of structures and mechanisms that bacteria use to regulate σ factor activity, reflecting the diversity of environmental cues that the bacterial transcription system has evolved to respond to.

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“…Rsd is known to bind to σ 70 with a stoichiometry of 1:1 and to function as an anti-sigma factor (18)(19)(20). The crystal structure of Rsd bound to region 4 of σ 70 indicates that Rsd binding directly interferes with both the core RNA polymerase-binding and promoter-binding functions of region 4 (21).…”

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confidence: 99%

HPr antagonizes the anti-σ ⁷⁰ activity of Rsd in Escherichia coli

Park

Lee

Choe

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) is a multicomponent system that participates in a variety of physiological processes in addition to the phosphorylation-coupled transport of numerous sugars. In Escherichia coli and other enteric bacteria, enzyme IIA Glc (EIIA Glc ) is known as the central processing unit of carbon metabolism and plays multiple roles, including regulation of adenylyl cyclase, the fermentation/respiration switch protein FrsA, glycerol kinase, and several non-PTS transporters, whereas the only known regulatory role of the E. coli histidine-containing phosphocarrier protein HPr is in the activation of glycogen phosphorylase. Because HPr is known to be more abundant than EIIA Glc in enteric bacteria, we assumed that there might be more regulatory mechanisms connected with HPr. The ligand fishing experiment in this study identified Rsd, an anti-sigma factor known to complex with σ 70 in stationary-phase cells, as an HPr-binding protein in E. coli. Only the dephosphorylated form of HPr formed a tight complex with Rsd and thereby inhibited complex formation between Rsd and σ 70. Dephosphorylated HPr, but not phosphorylated HPr, antagonized the inhibitory effect of Rsd on σ 70-dependent transcriptions both in vivo and in vitro, and also influenced the competition between σ 70 and σ S for core RNA polymerase in the presence of Rsd. Based on these data, we propose that the anti-σ 70 activity of Rsd is regulated by the phosphorylation state-dependent interaction of HPr with Rsd.glucose signaling | sigma factor competition | transcriptional regulation B y monitoring their environment, bacteria ensure the most appropriate response for each environment. One of the sensory systems for monitoring changes in nutrient availability is the phosphoenolpyruvate (PEP):sugar phosphotransferase system (PTS). The PTS is a multicomponent system that catalyzes the concomitant phosphorylation and translocation of numerous sugar substrates across the cytoplasmic membrane. This system consists of two general components, enzyme I (EI) and the histidine-containing phosphocarrier protein HPr, which are common to all PTS sugars, along with many sugar-specific components collectively known as enzyme IIs (EIIs) (1, 2).Each EII complex generally consists of three domains: one integral membrane domain forming the sugar translocation channel (EIIC) and two cytosolic domains (EIIA and EIIB). EI transfers a phosphoryl group from PEP to HPr, and HPr then transfers the phosphoryl group to the different EIIs. Each EII complex forms a cascade of phosphorylated intermediates, and in the presence of a PTS sugar, the EIIA and EIIB domains sequentially transfer the phosphate group from HPr to the incoming sugar. Thus, the phosphorylation states of the PTS components change depending on the availability of a PTS sugar substrate (3, 4).In addition to sugar uptake, the PTS plays an important role as a sensory transduction system to monitor nutritional changes, and its components are involved in the regula...

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Crystal Structure of the Escherichia coli Regulator of σ70, Rsd, in Complex with σ70 Domain 4

Cited by 57 publications

References 47 publications

Bacteriophage T4 MotA Activator and the β-Flap Tip of RNA Polymerase Target the Same Set of σ70 Carboxyl-terminal Residues

Bacteriophage T4 MotA Activator and the β-Flap Tip of RNA Polymerase Target the Same Set of σ70 Carboxyl-terminal Residues

Regulation of bacterial RNA polymerase σ factor activity: a structural perspective

HPr antagonizes the anti-σ ⁷⁰ activity of Rsd in Escherichia coli

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Crystal Structure of the Escherichia coli Regulator of σ70, Rsd, in Complex with σ70 Domain 4

Cited by 57 publications

References 47 publications

Bacteriophage T4 MotA Activator and the β-Flap Tip of RNA Polymerase Target the Same Set of σ70 Carboxyl-terminal Residues

Bacteriophage T4 MotA Activator and the β-Flap Tip of RNA Polymerase Target the Same Set of σ70 Carboxyl-terminal Residues

Regulation of bacterial RNA polymerase σ factor activity: a structural perspective

HPr antagonizes the anti-σ 70 activity of Rsd in Escherichia coli

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HPr antagonizes the anti-σ ⁷⁰ activity of Rsd in Escherichia coli