ArticleScientific reports2014
Thermal-triggerd proteinquake leads to disassembly of DegP hexamer as an imperative activation step.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Article
- The mechanism for thermal-enhanced chaperone-like activity of α-crystallin against UV irradiation-induced aggregation of γD-crystallin.Biophysical journal · 2022Article
- Structural basis of DegP protease temperature-dependent activation.Science advances · 2021Article
- Stress-Responsive Periplasmic Chaperones in Bacteria.Frontiers in molecular biosciences · 2021Review
- Dynamical and allosteric regulation of photoprotection in light harvesting complex II.Science China. Chemistry · 2020Article
- Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser.Nature communications · 2015Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli DegP has been reported to function both as molecular chaperone and protease for the quality control of outer membrane protein biogenesis. Activation of the inactive DegP hexamers was believed to occur via their disassembly into trimeric units and subsequent reassembly into larger oligomers (12-mers and 24-mers). Here, we analyzed the thermal stability and the unfolding dynamics of the different secondary structure components of the DegP hexamers using Fourier transform infrared spectroscopy and temperature-jump nanosecond time-resolved IR difference absorbance spectroscopy. We found that the interfacial secondary structure components possess a degreed thermal stability, with the disassembly of the DegP hexamers follows a "proteinquake" manner, such that the fully exposed parts of the interfacial β-sheets serving as the temperature sensor and epicenter to drive the sequential unfolding/disassembly process that finishes within about 134 ns at room temperature.
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Registered trials
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