A two-subunit bacterial σ-factor activates transcription in
            <i>Bacillus subtilis</i>

MacLellan, Shawn R.; Guariglia-Oropeza, Veronica; Gaballa, Ahmed; Helmann, John D.

doi:10.1073/pnas.0910006106

Cited by 16 publications

(21 citation statements)

References 40 publications

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“…4). Consistent with previously analyses (MacLellan et al, 2009a), SigO and the N-terminal half of SigO interact with RsoA (Fig. 4a).…”

Section: Rsio Competes With Rsoa For Interaction With Sigosupporting

confidence: 79%

“…Consistent with previous results using E. coli as a host and with activity in the native host B. subtilis (MacLellan et al, 2009a), co-expression of SigO and RsoA is required to initiate transcription from a P oxdC -gfp fusion (Fig. 2a).…”

Section: Genetic Organization Of the Sigo -Rsoa Regulonsupporting

confidence: 78%

“…In some cases, SigO was bisected to produce N-terminal and C-terminal fusions to CyaA. The full-length SigO protein is 176 amino acids in length and the N-terminal fragment tested consisted of the first 93 amino acids, a moiety we have previously shown specifically interacts with RsoA in vivo and in vitro (MacLellan et al, 2009a). The C-terminal SigO fragment tested consisted of amino acids 94-176.…”

Section: Methodsmentioning

confidence: 99%

“…1a) (MacLellan et al, 2008(MacLellan et al, , 2009a. Previous work demonstrated that deletion of the gene downstream of oxdC (rsiO, formerly yvrL) resulted in an increase in basal SigO-RsoA activity (MacLellan et al, 2008) and increased OxdC accumulation in B. subtilis cells (MacLellan et al, 2009b) suggesting that RsiO, a predicted membrane protein (Fig.…”

Section: Genetic Organization Of the Sigo -Rsoa Regulonmentioning

confidence: 99%

“…SigO-RsoA is an atypical two-subunit s factor from B. subtilis (MacLellan et al, 2008(MacLellan et al, , 2009a. Both proteins possess sequence similarity to the ECF s 70 family of proteins, interact with each other and with RNAP subunits, and are required for the initiation of transcription from a set of related promoters in the B. subtilis genome (MacLellan et al, 2009a, b).…”

Section: Introductionmentioning

confidence: 99%

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The atypical two-subunit σ factor from Bacillus subtilis is regulated by an integral membrane protein and acid stress

2016

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The atypical two-subunit s factor from Bacillus subtilis is regulated by an integral membrane protein and acid stress Extracytoplasmic function (ECF) s factors constitute a major component of the physicochemical sensory apparatus in bacteria. Most ECF s factors are co-expressed with a negative regulator called an anti-s factor that binds to its cognate s factor and sequesters it from productive association with core RNA polymerase (RNAP). Anti-s factors constitute an important element of signal transduction pathways that mediate an appropriate transcriptional response to changing environmental conditions. The Bacillus subtilis genome encodes seven canonical ECF s factors and six of these are co-expressed with experimentally verified anti-s factors. B. subtilis also expresses an ECF-like atypical two-subunit s factor composed of subunits SigO and RsoA that becomes active after exposure to certain cell-wall-acting antibiotics and to growth under acidic conditions. This work describes the identification and preliminary characterization of a protein (RsiO, formerly YvrL) that constitutes the anti-s factor cognate to SigO-RsoA. Synthesis of RsiO represses SigO-RsoA-dependent transcription initiation by binding the N-terminus of SigO under neutral (pH 7) conditions. Reconstitution of the SigO-RsoA-RsiO regulatory system into a heterologous host reveals that the imposition of acid stress (pH 5.4) abolishes the ability of RsiO to repress SigO-RsoA-dependent transcription and this correlates with loss of RsiO binding affinity for SigO. A current model for RsiO function indicates that RsiO responds, either directly or indirectly, to increased extracytoplasmic hydrogen ion concentration and becomes inactivated. This results in the release of SigO into the cytoplasm, where it productively associates with RsoA and core RNAP to initiate transcription from target promoters in the cell.

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“…4). Consistent with previously analyses (MacLellan et al, 2009a), SigO and the N-terminal half of SigO interact with RsoA (Fig. 4a).…”

Section: Rsio Competes With Rsoa For Interaction With Sigosupporting

confidence: 79%

Section: Genetic Organization Of the Sigo -Rsoa Regulonsupporting

confidence: 78%

Section: Methodsmentioning

confidence: 99%

Section: Genetic Organization Of the Sigo -Rsoa Regulonmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The atypical two-subunit σ factor from Bacillus subtilis is regulated by an integral membrane protein and acid stress

2016

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Bacillus subtilis

Harwood

Pohl

Smith

et al. 2013

Methods in Microbiology

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Recent Advances of Oxalate Decarboxylase: Biochemical Characteristics, Catalysis Mechanisms, and Gene Expression and Regulation

Zan,

Yan,

Chen

et al. 2024

J. Agric. Food Chem.

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Oxalate decarboxylase (OXDC) is a typical Mn 2+ /Mn 3+ dependent metal enzyme and splits oxalate to formate and CO 2 without any organic cofactors. Fungi and bacteria are the main organisms expressing the OXDC gene, but with a significantly different mechanism of gene expression and regulation. Many articles reported its potential applications in the clinical treatment of hyperoxaluria, low-oxalate food processing, degradation of oxalate salt deposits, oxalate acid diagnostics, biocontrol, biodemulsifier, and electrochemical oxidation. However, some questions still remain to be clarified about the role of substrate binding and/or protein environment in modulating the redox properties of enzyme-bound Mn(II)/Mn(III), the nature of dioxygen involved in the catalytic mechanism, and how OXDC acquires Mn(II) /Mn(III). This review mainly summarizes its biochemical and structure characteristics, gene expression and regulation, and catalysis mechanism. We also deep-mined oxalate decarboxylase gene data from National Center for Biotechnology Information to give some insights to explore new OXDC with diverse biochemical properties.

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A two-subunit bacterial σ-factor activates transcription in Bacillus subtilis

Cited by 16 publications

References 40 publications

The atypical two-subunit σ factor from Bacillus subtilis is regulated by an integral membrane protein and acid stress

The atypical two-subunit σ factor from Bacillus subtilis is regulated by an integral membrane protein and acid stress

Bacillus subtilis

Recent Advances of Oxalate Decarboxylase: Biochemical Characteristics, Catalysis Mechanisms, and Gene Expression and Regulation

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