Intrinsically disordered proteins articles within Nature Communications

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  • Article
    | Open Access

    Avian influenza polymerase undergoes host adaptation in order to efficiently replicate in human cells. Here, the authors use NMR spectroscopy and quantitative ensemble modelling to describe the highly dynamic assemblies formed by the human-adapted or avian-adapted C-terminal domains with the respective ANP32A host proteins.

    • Aldo R. Camacho-Zarco
    • , Sissy Kalayil
    •  & Martin Blackledge

  • Article
    | Open Access

    Three-colour FRET is a powerful tool to study macromolecular conformational dynamics, but is temporally limited due to the experimental complexity. Here the authors develop experimental and analytical methods for probing submillisecond-time scale dynamics using single continuous-wave excitation.

    • Janghyun Yoo
    • , Jae-Yeol Kim
    •  & Hoi Sung Chung

  • Article
    | Open Access

    Phosphorylation of eIF4E binding proteins (4E-BPs) controls their folding and regulates cap-dependent translation. Here, the authors show that phosphorylation of the C-terminal disordered region stabilizes the non-cooperatively folded 4E-BP domain to an eIF4E binding-incompatible state to control translation.

    • Jennifer E. Dawson
    • , Alaji Bah
    •  & Julie D. Forman-Kay

  • Article
    | Open Access

    In Parkinson’s disease (PD) the monomeric protein alpha-synuclein (aSyn) misfolds and aggregates into insoluble fibrils. Here the authors use NMR measurements and hydrogen–deuterium exchange mass spectrometry and find that the more solvent exposed the N-terminus of aSyn is, the more aggregation prone its conformation becomes, and further show how PD mutations and post translational modifications influence the extent of the N-terminus solvent exposure.

    • Amberley D. Stephens
    • , Maria Zacharopoulou
    •  & Gabriele S. Kaminski Schierle

  • Article
    | Open Access

    The production of microparticles with complex geometries for biotechnological use historically requires sophisticated fabrication techniques. Here, the authors create complex particle geometries by exploiting the metastable region of the phase diagram of thermally responsive intrinsically disordered proteins within microdroplets.

    • Stefan Roberts
    • , Vincent Miao
    •  & Ashutosh Chilkoti

  • Article
    | Open Access

    Galectin-3 consists of an unstructured N-terminal domain (NTD) and a structured carbohydrate-recognition domain and agglutinates neutrophils and glycosylated molecules in the extracellular milieu. Here the authors combine biophysical and biochemical experiments with NMR measurements and show that the galectin-3 NTD undergoes liquid-liquid phase separation (LLPS) and agglutinates other molecules through this process.

    • Yi-Ping Chiu
    • , Yung-Chen Sun
    •  & Jie-rong Huang

  • Article
    | Open Access

    Processing bodies are membrane less organelles that contain enzymes involved in mRNA turnover, among them enhancer of decapping 3 (Edc3). Here the authors use solid- and solution-state NMR spectroscopy to characterize the structural organization and dynamics of Edc3 and find that its interactions with RNA and between the different Edc3 domains are largely preserved in the phase-separated state.

    • Reinier Damman
    • , Stefan Schütz
    •  & Marc Baldus

  • Article
    | Open Access

    The biophysical mechanisms of how disease-associated tau mutations drive amyloid formation are not well understood. Here the authors use biophysical approaches, cell models and MD simulations and find that the intrinsically disordered repeat domain of tau encodes a metastable local structure and perturbations through mutations and proline isomerization cause an aggregation phenotype in vitro and in cells.

    • Dailu Chen
    • , Kenneth W. Drombosky
    •  & Lukasz A. Joachimiak

  • Article
    | Open Access

    RNA chaperones, such as the hepatitic C virus (HCV) core protein, are proteins that aid in the folding of nucleic acids. Here authors use single‐molecule spectroscopy and simulation to show that the HCV core protein acts as a flexible macromolecular counterion which facilitates nucleic acid folding.

    • Erik D. Holmstrom
    • , Zhaowei Liu
    •  & Benjamin Schuler

  • Article
    | Open Access

    Polyglutamine (polyQ) tracts are low-complexity regions and their expansion is linked to certain neurodegenerative diseases. Here the authors combine experimental and computational approaches to find that the length of the androgen receptor polyQ tract correlates with its helicity and show that the polyQ helical structure is stabilized by hydrogen bonds between the Gln side chains and main chain carbonyl groups.

    • Albert Escobedo
    • , Busra Topal
    •  & Xavier Salvatella

  • Article
    | Open Access

    The Pseudomonas putida toxin GraT and antitoxin GraA form a type II toxin-antoxin module. Here the authors present the crystal structures of the GraA dimer, GraTA and GraA-DNA complexes and show that GraT contains a functionally important N-terminal intrinsic disordered region that prevents the binding of the GraTA complex to the operator.

    • Ariel Talavera
    • , Hedvig Tamman
    •  & Remy Loris

  • Article
    | Open Access

    The microalgal pyrenoid has been reported to behave as a phase-separated liquid compartment. Here the authors demonstrate that the CO2-fixing enzyme Rubisco and the linker protein EPYC1 are necessary and sufficient to bring about a liquid-liquid phase separation that recapitulates the pyrenoid’s liquid-like behavior.

    • Tobias Wunder
    • , Steven Le Hung Cheng
    •  & Oliver Mueller-Cajar

  • Article
    | Open Access

    The nucleolus is a membrane-less organelle and both Nucleophosmin (NPM1) and Surfeit locus protein 6 (SURF6) are abundant proteins within the nucleolus. Here the authors employ biophysical methods to study the properties of NPM1-S6N droplets and provide insights into the role of SURF6 in maintaining and modulating the liquid-like structure of the nucleolus.

    • Mylene C. Ferrolino
    • , Diana M. Mitrea
    •  & Richard W. Kriwacki

  • Article
    | Open Access

    How interactions between binding partners form or break is hidden in the transition paths from the encounter to the formation of a stable complex. Here authors use single‐molecule spectroscopy to measure the transition path times for the association of two intrinsically disordered proteins that form a folded dimer upon binding and identify a metastable encounter complex.

    • Flurin Sturzenegger
    • , Franziska Zosel
    •  & Benjamin Schuler

  • Article
    | Open Access

    Intrinsically disordered proteins (IDPs) usually fold during binding to target proteins which involves the formation of a transient complex (TC). Here authors use single-molecule FRET to show that the lifetime of TC for IDP binding is very long due to the stabilization by non-native electrostatic interactions, which makes fast association possible.

    • Jae-Yeol Kim
    • , Fanjie Meng
    •  & Hoi Sung Chung

  • Article
    | Open Access

    Designer organelles with new biochemical functionalities are of great interest in synthetic biology and cellular engineering. Here the authors present a single-protein-based platform for generating synthetic membraneless compartments that is capable of enzymatically-triggered alterations to phase behavior and of recruiting and concentrating cargo proteins.

    • Benjamin S. Schuster
    • , Ellen H. Reed
    •  & Daniel A. Hammer

  • Article
    | Open Access

    The nucleolus is a membrane-less organelle formed through liquid–liquid phase separation (LLPS). Here the authors use biophysical methods and show that the nucleolar protein nucleophosmin (NPM1) also undergoes LLPS through homotypic, inter-NPM1 interactions and discuss implications for the ribosome biogenesis process.

    • Diana M. Mitrea
    • , Jaclyn A. Cika
    •  & Richard W. Kriwacki

  • Article
    | Open Access

    The Alzheimer protein Tau interacts with biological membranes, but the role of these interactions in regulating Tau function in health and disease remains unexplored. Here, the authors report on the discovery and characterization of neurotoxic oligomeric protein/phospholipid complexes.

    • Nadine Ait-Bouziad
    • , Guohua Lv
    •  & Hilal A. Lashuel

  • Article
    | Open Access

    Silk fibres currently used in biotechnology are chemically reconstituted silk fibroins (RSF), which are more stable than native silk fibroin (NSF) but possess different biophysical properties. Here, the authors use microfluidic droplets to encapsulate and store NSF, preserving their native structure.

    • Ulyana Shimanovich
    • , Francesco S. Ruggeri
    •  & Tuomas P. J. Knowles

  • Article
    | Open Access

    Huntington's disease is caused by a polyglutamine stretch expansion in the first exon of huntingtin. Here, the authors use infrared spectroscopy and solid-state NMR and show that polymorphic huntingtin exon1 fibres differ in their flanking regions but not their core polyglutamine amyloid structures.

    • Hsiang-Kai Lin
    • , Jennifer C. Boatz
    •  & Patrick C. A. van der Wel

  • Article
    | Open Access

    The RNA polymerase II C-terminal domain acts as a hub to coordinate transcription and nascent mRNA processing. Here the authors identify a phosphorylation-dependent switch in thetrans-to-cisisomerization of proline in the CTD heptad repeats that make those repeats susceptible to further modifications by regulatory enzymes.

    • Eric B. Gibbs
    • , Feiyue Lu
    •  & Scott A. Showalter

  • Article
    | Open Access

    The WD40 domain of the SCFCdc4ubiquitin ligase targets substrates via multiple phosphorylated degron motifs. The authors define a second degron-binding WD40 pocket that imparts a negative allosteric effect on binding to the primary pocket, and thereby enables the dynamic exchange of bound degrons.

    • Veronika Csizmok
    • , Stephen Orlicky
    •  & Julie D. Forman-Kay

  • Article
    | Open Access

    The elucidation of amyloid nucleation mechanisms remains challenging as early oligomeric intermediates are transient and difficult to distinguish. Here the authors use Aβ- polyglutamine hybrid peptides designed to slow and limit amyloid maturation to provide insights into the structures of Aβ self-assembly intermediates.

    • Pinaki Misra
    • , Ravindra Kodali
    •  & Ronald Wetzel

  • Article
    | Open Access

    Intrinsically disordered proteins can phase separate from the soluble intracellular space. Here the authors show that the nucleic acid-mimicking biopolymer poly(ADP-ribose) (PAR) nucleates intracellular liquid demixing and orchestrates the earliest cellular responses to DNA breakage.

    • Matthias Altmeyer
    • , Kai J. Neelsen
    •  & Jiri Lukas

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