ArticleProceedings of the National Academy of Sciences of the United States of America2015
Steric clashes with bound OMP peptides activate the DegS stress-response protease.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- DegS regulates the aerobic metabolism ofFrontiers in cellular and infection microbiology · 2024Article
- Fever-like temperature bursts promote competence development via an HtrA-dependent pathway in Streptococcus pneumoniae.PLoS genetics · 2023Article
- DegS protease regulates antioxidant capacity and adaptability to oxidative stress environment inFrontiers in cellular and infection microbiology · 2023Article
- DegS protease regulates the motility, chemotaxis, and colonization ofFrontiers in microbiology · 2023Article
- Role of Regulated Proteolysis in the Communication of Bacteria With the Environment.Frontiers in molecular biosciences · 2020Review
- Fine-Tuning of σJournal of bacteriology · 2019Article
- A Multireporter Bacterial 2-Hybrid Assay for the High-Throughput and Dynamic Assay of PDZ Domain-Peptide Interactions.ACS synthetic biology · 2019Article
- Exploration of the effects of aPeerJ · 2019Article
- HtrA1 activation is driven by an allosteric mechanism of inter-monomer communication.Scientific reports · 2017Article
- Two stress sensor proteins for the expression of sigmaE regulon: DegS and RseB.Journal of microbiology (Seoul, Korea) · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Escherichia coli senses envelope stress using a signaling cascade initiated when DegS cleaves a transmembrane inhibitor of a transcriptional activator for response genes. Each subunit of the DegS trimer contains a protease domain and a PDZ domain. During stress, unassembled outer-membrane proteins (OMPs) accumulate in the periplasm and their C-terminal peptides activate DegS by binding to its PDZ domains. In the absence of stress, autoinhibitory interactions, mediated by the L3 loop, stabilize inactive DegS, but it is not known how this autoinhibition is reversed during activation. Here, we show that OMP peptides initiate a steric clash between the PDZ domain and the L3 loop that results in a structural rearrangement of the loop and breaking of autoinhibitory interactions. Many different L3-loop sequences are compatible with activation but those that relieve the steric clash reduce OMP activation dramatically. Our results provide a compelling molecular mechanism for allosteric activation of DegS by OMP-peptide binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.