Crystal Structure of Escherichia coli σE with the Cytoplasmic Domain of Its Anti-σ RseA

Campbell, Elizabeth A.; Tupy, Jonathan L.; Gruber, Tanja M.; Wang, Sheng; Sharp, Meghan M.; Gross, Carol A.; Darst, Seth A.

doi:10.1016/s1097-2765(03)00148-5

Cited by 228 publications

(300 citation statements)

References 66 publications

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“…This fragment is easy to purify because it is stable in E. coli. It is also sufficient for antiactivity both in vivo and in vitro (De Las Penas et al 1997b;Missiakas et al 1997;Campbell et al 2003). We used fluorescence anisotropy to measure the dissociation of rhodamine-labeled RseA 1-100 from E .…”

Section: The Cytoplasmic Domain Of Rsea Binds Very Tightly To Ementioning

confidence: 99%

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Design principles of the proteolytic cascade governing the σ^E-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction

Chaba¹,

Grigorova²,

Flynn³

et al. 2007

Genes Dev.

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104

119

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Proteolytic cascades often transduce signals between cellular compartments, but the features of these cascades that permit efficient conversion of a biological signal into a transcriptional output are not well elucidated. E mediates an envelope stress response in Escherichia coli, and its activity is controlled by regulated degradation of RseA, a membrane-spanning anti-factor. Examination of the individual steps in this protease cascade reveals that the initial, signal-sensing cleavage step is rate-limiting; that multiple ATP-dependent proteases degrade the cytoplasmic fragment of RseA and that dissociation of E from RseA is so slow that most free E must be generated by the active degradation of RseA. As a consequence, the degradation rate of RseA is set by the amount of inducing signal, and insulated from the "load" on and activity of the cytoplasmic proteases. Additionally, changes in RseA degradation rate are rapidly reflected in altered E activity. These design features are attractive as general components of signal transduction pathways governed by unstable negative regulators. Proteolytic cascades are widely used to transduce signals across membranes to enable cells to respond to environmental stress and coordinate processes in different cellular compartments. However, the molecular properties of these cascades that facilitate the desired outputs have rarely been examined. In this work, we examine the individual steps in the protease cascade governing the activity of the E -mediated envelope stress response in Escherichia coli to determine the construction features of this cascade that facilitate faithful transmission of signal and a rapid output.E directs RNA polymerase to transcribe genes encoding proteins that ensure the synthesis, assembly, and homeostasis of outer membrane porins and lipopolysaccharide, the two major components of the unique outer membrane of Gram-negative bacteria (Dartigalongue et al. 2001;Rezuchova et al. 2003;Rhodius et al. 2006). Envelope integrity is required under all growth conditions, and E is an essential transcription factor (De Las Penas et al. 1997a). Perturbations in the integrity and protein-folding state of the envelope caused by temperature upshift, chaperone depletion, or accumulation of unassembled porins increase E activity; conversely, temperature downshift and/or depletion of porins decrease E activity (Mecsas et al. 1993;Hiratsu et al. 1995;Raina et al. 1995;Rouviere et al. 1995;Missiakas et al. 1996;Rouviere and Gross 1996;Ades et al. 2003).The components of the signal transduction system that control E activity are shown in Figure 1. RseA, a membrane-spanning anti-factor, inhibits E activity. The cytoplasmic domain of RseA (RseA 1-108 ) binds to E and its periplasmic domain binds to RseB (De Las Penas et al. 1997b;Missiakas et al. 1997

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Section: The Cytoplasmic Domain Of Rsea Binds Very Tightly To Ementioning

confidence: 99%

“…The cytoplasmic domain of RseA (RseA 1-108 ) binds to E and its periplasmic domain binds to RseB (De Las Penas et al 1997b;Missiakas et al 1997). Interaction of E with RseA prevents E from binding to RNA polymerase (Campbell et al 2003). This inhibitory interaction is re-lieved when RseA is degraded via a proteolytic cascade.…”

mentioning

confidence: 99%

Design principles of the proteolytic cascade governing the σ^E-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction

Chaba¹,

Grigorova²,

Flynn³

et al. 2007

Genes Dev.

Self Cite

104

119

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“…5B) (Raivio and Silhavy, 2001;Alba and Gross, 2004). In that pathway, RseA is an anti-sigma factor with a central transmembrane segment whose N-terminal, cytoplasmic domain sequesters s E and represses its essential activity (De Las Penas et al, 1997;Missiakas et al, 1997;Ades et al, 1999;Campbell et al, 2003). When periplasmic protease…”

Section: Dicmentioning

confidence: 99%

A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant

Chen

Viollier

Shapiro

2005

Molecular Microbiology

123

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SummaryCaulobacter crescentus assembles many of its cellular machines at distinct times and locations during the cell cycle. PodJ provides the spatial cues for the biogenesis of several polar organelles, including the pili, adhesive holdfast and chemotactic apparatus, by recruiting structural and regulatory proteins, such as CpaE and PleC, to a specific cell pole. PodJ is a protein with a single transmembrane domain that exists in two forms, full-length (PodJ L ) and truncated (PodJ S ), each appearing during a specific time period of the cell cycle to control different aspects of polar organelle development. PodJ L is synthesized in the early predivisional cell and is later proteolytically converted to PodJ S . During the swarmer-to-stalked transition, PodJ S must be degraded to preserve asymmetry in the next cell cycle. We found that MmpA facilitates the degradation of PodJ S . MmpA belongs to the site-2 protease (S2P) family of membraneembedded zinc metalloproteases, which includes SpoIVFB and YluC of Bacillus subtilis and YaeL of Escherichia coli . MmpA appears to cleave within or near the transmembrane segment of PodJ S , releasing it into the cytoplasm for complete proteolysis. While PodJ S has a specific temporal and spatial address, MmpA is present throughout the cell cycle; furthermore, periplasmic fusion to mRFP1 suggested that MmpA is uniformly distributed around the cell. We also determined that mmpA and yaeL can complement each other in C. crescentus and E. coli , indicating functional conservation. Thus, the sequential degradation of PodJ appears to involve regulated intramembrane proteolysis (Rip) by MmpA.

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“…So how is the unfolded protein stress signal sensed and transmitted across the membrane? In the absence of stress, SigmaE is bound, with high affinity, to the cytoplasmic domain of the anti-sigma factor, regulator of SigmaE (RseA) thereby inhibiting its transcriptional activity (44)(45)(46)(47) (Fig. 2a).…”

Section: Proteolytic Control Of the Envelope Stress Response In E Colimentioning

confidence: 99%

“…This action results in the release of the cytoplasmic domain of RseA (RseA ) from the membrane (48,51,58,59). Interestingly, the release of RseA 1-108 from the membrane is insufficient for SigmaE release or transcription of the SigmaE regulon (44,45). Thus, the final step in the signal transduction pathway, that is, the degradation of RseA 1-108 to release SigmaE, requires the action of one of several cytoplasmic AAA1 proteases (36,45,50).…”

Section: Proteolytic Control Of the Envelope Stress Response In E Colimentioning

confidence: 99%

Unfolded protein responses in bacteria and mitochondria: A central role for the ClpXP machine

2011

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SummaryIn the crowded environment of a cell, the protein quality control machinery, such as molecular chaperones and proteases, maintains a population of folded and hence functional proteins. The accumulation of unfolded proteins in a cell is particularly harmful as it not only reduces the concentration of active proteins but also overburdens the protein quality control machinery, which in turn, can lead to a significant increase in nonproductive folding and protein aggregation. To circumvent this problem, cells use heat shock and unfolded protein stress response pathways, which essentially sense the change to protein homeostasis upregulating protein quality control factors that act to restore the balance. Interestingly, several stress response pathways are proteolytically controlled. In this review, we provide a brief summary of targeted protein degradation by AAA1 proteases and focus on the role of ClpXP proteases, particularly in the signaling pathway of the Escherichia coli extracellular stress response and the mitochondrial unfolded protein response. IUBMBIUBMB Life, 63(11): 955-963, 2011

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Crystal Structure of Escherichia coli σE with the Cytoplasmic Domain of Its Anti-σ RseA

Cited by 228 publications

References 66 publications

Design principles of the proteolytic cascade governing the σ^E-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction

Design principles of the proteolytic cascade governing the σ^E-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction

A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant

Unfolded protein responses in bacteria and mitochondria: A central role for the ClpXP machine

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Crystal Structure of Escherichia coli σE with the Cytoplasmic Domain of Its Anti-σ RseA

Cited by 228 publications

References 66 publications

Design principles of the proteolytic cascade governing the σE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction

Design principles of the proteolytic cascade governing the σE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction

A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant

Unfolded protein responses in bacteria and mitochondria: A central role for the ClpXP machine

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Design principles of the proteolytic cascade governing the σ^E-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction

Design principles of the proteolytic cascade governing the σ^E-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction