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Dynamic binding of the bacterial chaperone Trigger factor to translating ribosomes in .
Proc Natl Acad Sci U S A
January 2025
Department of Cell & Molecular Biology, Uppsala University, Uppsala SE-75124, Sweden.
The bacterial chaperone Trigger factor (TF) binds to ribosome-nascent chain complexes (RNCs) and cotranslationally aids the folding of proteins in bacteria. Decades of studies have given a broad, but often conflicting, description of the substrate specificity of TF, its RNC-binding dynamics, and competition with other RNC-binding factors, such as the Signal Recognition Particle (SRP). Previous RNC-binding kinetics experiments were commonly conducted on stalled RNCs in reconstituted systems, and consequently, may not be representative of the interaction of TF with ribosomes translating mRNA in the cytoplasm of the cell.
View Article and Find Full Text PDFTopological confinement by a membrane anchor suppresses phase separation into protein aggregates: Implications for prion diseases.
Proc Natl Acad Sci U S A
January 2025
Department Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, Bochum 44801, Germany.
Protein misfolding and aggregation are a hallmark of various neurodegenerative disorders. However, the underlying mechanisms driving protein misfolding in the cellular context are incompletely understood. Here, we show that the two-dimensional confinement imposed by a membrane anchor stabilizes the native protein conformation and suppresses liquid-liquid phase separation (LLPS) and protein aggregation.
View Article and Find Full Text PDFStress-inducible phosphoprotein 1 (Sti1/Stip1/Hop) sequesters misfolded proteins during stress.
FEBS J
December 2024
Department of Anatomy and Cell Biology, The University of Western Ontario, London, Canada.
Co-chaperones are key elements of cellular protein quality control. They cooperate with the major heat shock proteins Hsp70 and Hsp90 in folding proteins and preventing the toxic accumulation of misfolded proteins upon exposure to stress. Hsp90 interacts with the co-chaperone stress-inducible phosphoprotein 1 (Sti1/Stip1/Hop) and activator of Hsp90 ATPase protein 1 (Aha1) among many others.
View Article and Find Full Text PDFAssembly of Structurally Simple Icosahedral Viruses.
Subcell Biochem
December 2024
Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM) and Department of Molecular Biology, Universidad Autónoma de Madrid, Madrid, Spain.
Icosahedral viruses exhibit elegant pathways of capsid assembly and maturation regulated by symmetry principles. Assembly is a dynamic process driven by consecutive and genetically programmed morphogenetic interactions between protein subunits. The non-symmetric capsid subunits are gathered by non-covalent contacts and interactions in assembly intermediates, which serve as blocks to build a symmetric capsid.
View Article and Find Full Text PDFNoncanonical calcium binding motif controls folding of HopQ1, a Pseudomonas syringae type III secretion effector, in a pH-dependent manner.
Sci Rep
December 2024
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Virulence of many gram-negative bacteria relies upon delivery of type three effectors into host cells. To pass through the conduit of secretion machinery the effectors need to acquire an extended conformation, and in many bacterial species specific chaperones assist in this process. In plant pathogenic bacterium Pseudomonas syringae, secretion of only few effectors requires the function of chaperones.
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