Bacillus subtilis Intramembrane Protease RasP Activity in Escherichia coli and
            <i>In Vitro</i>

Parrell, Daniel; Zhang, Yang; Olenic, Sandra; Kroos, Lee

doi:10.1128/jb.00381-17

Cited by 12 publications

(10 citation statements)

References 51 publications

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“…FtsL protein levels are normally controlled through regulated intramembrane proteolysis (RIP). FtsL contains a cytoplasmic recognition motif that is cleaved by RasP, an intramembrane zinc metalloprotease (79,80). The DivIC protein stabilizes FtsL, preventing cleavage by RasP (81).…”

Section: Sos-independent Regulation Of Cell Divisionmentioning

confidence: 99%

Regulation of Cell Division in Bacteria by Monitoring Genome Integrity and DNA Replication Status

Burby

Simmons

2020

J Bacteriol

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All organisms regulate cell cycle progression by coordinating cell division with DNA replication status. In eukaryotes, DNA damage or problems with replication fork progression induce the DNA damage response (DDR), causing cyclin-dependent kinases to remain active, preventing further cell cycle progression until replication and repair are complete. In bacteria, cell division is coordinated with chromosome segregation, preventing cell division ring formation over the nucleoid in a process termed nucleoid occlusion. In addition to nucleoid occlusion, bacteria induce the SOS response after replication forks encounter DNA damage or impediments that slow or block their progression. During SOS induction, Escherichia coli expresses a cytoplasmic protein, SulA, that inhibits cell division by directly binding FtsZ. After the SOS response is turned off, SulA is degraded by Lon protease, allowing for cell division to resume. Recently, it has become clear that SulA is restricted to bacteria closely related to E. coli and that most bacteria enforce the DNA damage checkpoint by expressing a small integral membrane protein. Resumption of cell division is then mediated by membrane-bound proteases that cleave the cell division inhibitor. Further, many bacterial cells have mechanisms to inhibit cell division that are regulated independently from the canonical LexA-mediated SOS response. In this review, we discuss several pathways used by bacteria to prevent cell division from occurring when genome instability is detected or before the chromosome has been fully replicated and segregated.

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Section: Sos-independent Regulation Of Cell Divisionmentioning

confidence: 99%

Regulation of Cell Division in Bacteria by Monitoring Genome Integrity and DNA Replication Status

Burby

Simmons

2020

J Bacteriol

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“…RseP utilizes tandem PDZ domains to recognize substrates via a size filtering rather than recognizing a specific amino acid sequence (Hizukuri et al , ). RasP contains a single PDZ domain that is also thought to function as a size exclusion filter for substrates (Parrell et al , ). In E. faecalis Eep, a metalloprotease homologous to RasP (44% identity and 62% similarity) functions as the site‐2 protease and is required for RsiV degradation and σ V activation (Varahan et al , ).…”

Section: Degradation Of Rsivmentioning

confidence: 99%

Activation of the extracytoplasmic function σ factor σ^V by lysozyme

Ellermeier

2019

Molecular Microbiology

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σ V is an extracytoplasmic function (ECF) σ factor that is found exclusively in Firmicutes including Bacillus subtilis and the opportunistic pathogens Clostridioides difficile and Enterococcus faecalis. σ V is activated by lysozyme and is required for lysozyme resistance. The activity of σ V is normally inhibited by the anti-σ factor RsiV, a transmembrane protein. RsiV acts as a receptor for lysozyme. The binding of lysozyme to RsiV triggers a signal transduction cascade which results in degradation of RsiV and activation of σ V . Like the anti-σ factors for several other ECF σ factors, RsiV is degraded by a multistep proteolytic cascade that is regulated at the step of site-1 cleavage. Unlike other anti-σ factors, site-1 cleavage of RsiV is not dependent upon a site-1 protease whose activity is regulated. Instead constitutively active signal peptidase cleaves RsiV at site-1 in a lysozyme-dependent manner. The activation of σ V leads to the transcription of genes, which encode proteins required for lysozyme resistance. Extracytoplasmic function (ECF) σ factor backgroundECF σ factors belong to the σ 70 family of σ factors and contain only the σ 2 and σ 4.2 domains. These are homologous to the σ 70 σ 2 and σ 4.2 domains and are required for binding to the -35 and -10 regions of target promoters (Helmann, 2002;2016;Staroń et al., 2009). In addition, most ECF σ factors are required for their own expression. The activity of most ECF σ factors is inhibited by a cognate anti-σ factor which is often encoded within the σ factor operon. Many but not all anti-σ factors are membrane proteins (Staroń et al., 2009). The σ factor activity is induced by inhibiting the function of the anti-σ factor. Activation of the σ factor can occur by one of several mechanisms; a conformational change in the anti-σ factor releases the σ factor, an anti-anti-σ factor binds to the anti-σ factor inducing σ factor release, or destruction of the anti-σ factor via regulated intramembrane proteolysis (Ho and Ellermeier, 2012;Helmann, 2016). Here, we will focus on activation of ECF σ factors by degradation of the anti-σ factor. In the presence of an inducing signal, a site-1 protease cleaves the extracellular domain of an anti-σ factor. Following site-1 protease cleavage, the truncated anti-σ factor is cleaved by a site-2 protease within the transmembrane region of the anti-σ factor. The remainder of the anti-σ factor is then degraded by cytosolic proteases. This frees the σ factor to interact with RNA polymerase and transcribe target genes (Brown et al., 2000;Ho and Ellermeier, 2012;Helmann, 2016).The ECF σ factor σ V is found exclusively in Firmicutes or low GC Gram-positive bacteria and belongs to the ECF30 family of ECF σ factors (Staroń et al., 2009). The σ V system is encoded by the model organism Bacillus subtilis, as well as the opportunistic pathogens Enterococcus faecalis and Clostridioides difficile (Fig. 1). σ V is not present in all Firmicutes or even closely related species. While present in B. subtilis, σ V is not present in B. anthrac...

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“…The DegS-cleaved form of RseA, which has lost most of its periplasmic domain, can pass through the PDZ filter and gain access to the intramembrane active site of RseP. It has been suggested that the single PDZ domain of Bacillus subtilis S2P homolog, RasP, might also act as a sizeexclusion filter (Parrell et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

Involvement of a Membrane-Bound Amphiphilic Helix in Substrate Discrimination and Binding by an Escherichia coli S2P Peptidase RseP

2020

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Intramembrane proteases (IMPs) are a unique class of proteases that catalyze the proteolysis within the membrane and regulate diverse cellular processes in various organisms. RseP, an Escherichia coli site-2 protease (S2P) family IMP, is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-σE) protein RseA. Extracytoplasmic stresses trigger a sequential cleavage of RseA, in which first DegS cleaves off its periplasmic domain, and RseP catalyzes the second cleavage of RseA. The two tandem-arranged periplasmic PDZ (PDZ tandem) domains of RseP serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP IMP domain. However, RseP’s substrate recognition mechanism is not fully understood. Here, we found that a periplasmic region of RseP, located downstream of the PDZ tandem, contains a segment (named H1) predicted to form an amphiphilic helix. Bacterial S2P homologs with various numbers of PDZ domains have a similar amphiphilic helix in the corresponding region. We demonstrated that the H1 segment forms a partially membrane-embedded amphiphilic helix on the periplasmic surface of the membrane. Systematic and random mutagenesis analyses revealed that the H1 helix is important for the stability and proteolytic function of RseP and that mutations in the H1 segment can affect the PDZ-mediated substrate discrimination. Cross-linking experiments suggested that H1 directly interacts with the DegS-cleaved form of RseA. We propose that H1 acts as an adaptor required for proper arrangement of the PDZ tandem domain to perform its filter function and for substrate positioning for its efficient cleavage.

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Bacillus subtilis Intramembrane Protease RasP Activity in Escherichia coli and In Vitro

Cited by 12 publications

References 51 publications

Regulation of Cell Division in Bacteria by Monitoring Genome Integrity and DNA Replication Status

Regulation of Cell Division in Bacteria by Monitoring Genome Integrity and DNA Replication Status

Activation of the extracytoplasmic function σ factor σ^V by lysozyme

Involvement of a Membrane-Bound Amphiphilic Helix in Substrate Discrimination and Binding by an Escherichia coli S2P Peptidase RseP

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Bacillus subtilis Intramembrane Protease RasP Activity in Escherichia coli and In Vitro

Cited by 12 publications

References 51 publications

Regulation of Cell Division in Bacteria by Monitoring Genome Integrity and DNA Replication Status

Regulation of Cell Division in Bacteria by Monitoring Genome Integrity and DNA Replication Status

Activation of the extracytoplasmic function σ factor σV by lysozyme

Involvement of a Membrane-Bound Amphiphilic Helix in Substrate Discrimination and Binding by an Escherichia coli S2P Peptidase RseP

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Activation of the extracytoplasmic function σ factor σ^V by lysozyme