ClpG is a novel autonomous disaggregase found in Pseudomonas aeruginosa that confers resistance to lethal heat stress. The mechanism by which ClpG specifically targets protein aggregates for disaggregation is unknown. In their recent work published in JBC, Katikaridis et al. (2023) identify an avidity-based mechanism by which four or more ClpG subunits, through specific N-terminal hydrophobic residues located on an exposed β-sheet loop, interact with multiple hydrophobic patches on an aggregated protein substrate. This study establishes a model for substrate binding to a prokaryotic disaggregase that should inform further investigations into other autonomous disaggregases.
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http://dx.doi.org/10.1016/j.jbc.2024.107165 | DOI Listing |
J Biol Chem
April 2024
Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada; Department of Chemistry, University of Toronto, Toronto, Ontario, Canada. Electronic address:
ClpG is a novel autonomous disaggregase found in Pseudomonas aeruginosa that confers resistance to lethal heat stress. The mechanism by which ClpG specifically targets protein aggregates for disaggregation is unknown. In their recent work published in JBC, Katikaridis et al.
View Article and Find Full Text PDFMaterials (Basel)
May 2022
School of Information and Electronic Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, China.
We propose an all-fiber broadband circular polarizer based on leaky mode coupling and a phase-matched turning point (PMTP) in a chirped, double-helix, chiral, long-period, fiber grating (CLPG). The CLPG was coated with a material in which the refractive index was higher than that of the fiber cladding, enabling the coupling of the core mode to leaky modes to achieve a desired extinction ratio. The complex coupled-mode theory was employed to investigate the coupling mechanism and conditions under which the desired coupling efficiency could be achieved.
View Article and Find Full Text PDFMicrob Pathog
February 2022
Instituto Nacional de Tecnología Agropecuaria (INTA), Instituto de Innovación para la Producción Agropecuaria y Desarrollo Sostenible, INTA-Consejo Nacional de Investigaciones Científicas y Técnicas (IPADS, INTA-CONICET), Ruta 226 km 73.5, Balcarce, 7620, Buenos Aires, Argentina.
Escherichia coli is an important cause of septicemia (SEPEC) and neonatal meningitis (NMEC) in dairy calves. However, the diversity of virulence profiles, phylogroups, antimicrobial resistance patterns, carriage of integron structures, and fluoroquinolone (FQ) resistance mechanisms have not been fully investigated. Also, there is a paucity of knowledge about the virulence profiles and frequency of potential SEPEC in feces from calves with or without diarrhea.
View Article and Find Full Text PDFFront Mol Biosci
May 2021
Center for Molecular Biology of the Heidelberg University and German Cancer Research Center, DKFZ-ZMBH Alliance, Heidelberg, Germany.
Bacteria as unicellular organisms are most directly exposed to changes in environmental growth conditions like temperature increase. Severe heat stress causes massive protein misfolding and aggregation resulting in loss of essential proteins. To ensure survival and rapid growth resume during recovery periods bacteria are equipped with cellular disaggregases, which solubilize and reactivate aggregated proteins.
View Article and Find Full Text PDFJ Biol Chem
August 2021
Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany; German Cancer Research Center (DKFZ), A250 Chaperones and Proteases, Heidelberg, Germany. Electronic address:
Bacterial survival during lethal heat stress relies on the cellular ability to reactivate aggregated proteins. This activity is typically executed by the canonical 70-kDa heat shock protein (Hsp70)-ClpB bichaperone disaggregase, which is most widespread in bacteria. The ClpB disaggregase is a member of the ATPase associated with diverse cellular activities protein family and exhibits an ATP-driven threading activity.
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