Temperature-induced conformational changes within the regulatory loops L1–L2–LA of the HtrA heat-shock protease from Escherichia coli

Sobiecka-Szkatula, Anna; Polit, Agnieszka; Scirè, Andrea; Giełdoń, Artur; Tanfani, Fabio; Szkarlat, Zaneta; Ciarkowski, Jerzy; Żurawa-Janicka, Dorota; Skórko-Glonek, Joanna; Lipińska, Barbara

doi:10.1016/j.bbapap.2009.07.002

Cited by 19 publications

(34 citation statements)

References 32 publications

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“…2c) can be assigned to be produced from β-sheets in general, while the other peaks can be assigned to be produced from loops/helices (1651 cm −1 ), turns (1666 cm −1 ), and the high frequency vibration of anti-parallel β-sheets (1678 cm −1 and 1683 cm −1 ). Our secondary structure assignments of the major peaks are largely consistent to those reported earlier1112. The simultaneous appearance of absorption at 1618 cm −1 and 1683 cm −1 at temperatures higher than 70°C (Fig.…”

Section: Resultssupporting

confidence: 90%

Thermal-triggerd Proteinquake Leads to Disassembly of DegP Hexamer as an Imperative Activation Step

Wang

et al. 2014

Sci Rep

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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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Section: Resultssupporting

confidence: 90%

Thermal-triggerd Proteinquake Leads to Disassembly of DegP Hexamer as an Imperative Activation Step

Wang

et al. 2014

Sci Rep

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“…12 and this work). The overall structural changes within the proteolytic domain occur in parallel (12). Furthermore, the dynamic light scattering analysis indicates that the diameter of the HtrA hexamer increases with an increase in temperature, suggesting loosening of the oligomer structure (not shown).…”

Section: Discussionmentioning

confidence: 95%

“…The plasmids pJS13 or pJS14, pJSFW, or pJS19 were used as templates to generate the pDF plasmids (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18) or the pMD2, pJSFW, and the pDF 21A, pDF19A, or pDF (20A, 22A) plasmid, respectively. The oligonucleotide primers used for mutagenesis were designed according to the QuikChange mutagenesis kit protocol and are listed in supplemental Table S2.…”

Section: Methodsmentioning

confidence: 99%

“…Steady-state fluorescence, fluorescence quenching, and time-resolved fluorescence decay measurements were carried out as described in Sobiecka-Szkatula et al (12).…”

Section: Methodsmentioning

confidence: 99%

“…It gradually becomes solvent-exposed, and the extent of this conformational change is both proportional and correlated to the increase of temperature effectuated (starting from 25°C) and to the degree of HtrA proteolytic activity stimulated. The remaining loops (L2 and L1) change their conformation at higher temperatures (above 35°C or 40°C, respectively) (12).…”

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confidence: 99%

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The LA Loop as an Important Regulatory Element of the HtrA (DegP) Protease from Escherichia coli

Figaj

Giełdoń

Polit

et al. 2014

Journal of Biological Chemistry

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Background: An understanding of the HtrA protease activation mechanism is incomplete with respect to its LA regulatory loop.Results: A theoretical model of the LA structure is provided and experimentally verified. Conclusion: LA intersubunit contacts strongly contribute to the stabilization of the inactive HtrA. Significance: This is the first report that simultaneously offers a theoretical three-dimensional structure of LA and its biophysical and functional properties.

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Characterization of Thymoquinone Binding to Human α1-Acid Glycoprotein

Lupidi

Camaioni

Khalifé

et al. 2012

Journal of Pharmaceutical Sciences

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Temperature-induced conformational changes within the regulatory loops L1–L2–LA of the HtrA heat-shock protease from Escherichia coli

Cited by 19 publications

References 32 publications

Thermal-triggerd Proteinquake Leads to Disassembly of DegP Hexamer as an Imperative Activation Step

Thermal-triggerd Proteinquake Leads to Disassembly of DegP Hexamer as an Imperative Activation Step

The LA Loop as an Important Regulatory Element of the HtrA (DegP) Protease from Escherichia coli

Characterization of Thymoquinone Binding to Human α1-Acid Glycoprotein

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