Molecular Principles of the Interactions of Disordered Proteins

Mészáros, Bálint; Tompa, Péter; Simon, István; Dosztányi, Zsuzsanna

doi:10.1016/j.jmb.2007.07.004

Cited by 250 publications

(299 citation statements)

References 55 publications

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“…It should be noted that the small negative peak at approximately 224 nm suggests some residual helical content in both proteins. When ERD10 and ERD14 were titrated with trifluoro acetic acid (data not shown), a transition from the disordered state to the helix was observed within the range of 15% to 30% trifluoro acetic acid, which suggests a significant local preference for the helical conformation and a possible induced folding mechanism during interaction with partners (Johansson et al, 2003;Meszaros et al, 2007). In all, these observations unequivocally suggest that ERD10 and ERD14 are highly disordered proteins.…”

Section: Idp Character Of Erd10 and Erd14mentioning

confidence: 78%

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

et al. 2008

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ERD10 and ERD14 (for early response to dehydration) proteins are members of the dehydrin family that accumulate in response to abiotic environmental stresses, such as high salinity, drought, and low temperature, in Arabidopsis (Arabidopsis thaliana). Whereas these proteins protect cells against the consequences of dehydration, the exact mode(s) of their action remains poorly understood. Here, detailed evidence is provided that ERD10 and ERD14 belong to the family of intrinsically disordered proteins, and it is shown in various assays that they act as chaperones in vitro. ERD10 and ERD14 are able to prevent the heat-induced aggregation and/or inactivation of various substrates, such as lysozyme, alcohol dehydrogenase, firefly luciferase, and citrate synthase. It is also demonstrated that ERD10 and ERD14 bind to acidic phospholipid vesicles without significantly affecting membrane fluidity. Membrane binding is strongly influenced by ionic strength. Our results show that these intrinsically disordered proteins have chaperone activity of rather wide substrate specificity and that they interact with phospholipid vesicles through electrostatic forces. We suggest that these findings provide the rationale for the mechanism of how these proteins avert the adverse effects of dehydration stresses.

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Section: Idp Character Of Erd10 and Erd14mentioning

confidence: 78%

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

et al. 2008

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“…HCA is similarly instrumental for the identification of regions undergoing induced folding, as buried hydrophobic residues at the protein-partner interface are often the major driving force in protein folding. 163,166 In some cases, hydrophobic clusters are found within secondary structure elements that are unstable in the native protein, but can stably fold upon binding to a partner. Therefore, HCA can be very useful to highlight potential induced folding regions (for examples see refs.…”

Section: Identifying Regions Of Induced Foldingmentioning

confidence: 99%

How disordered is my protein and what is its disorder for? A guide through the “dark side” of the protein universe

Lieutaud

Ferrón

Uversky

et al. 2016

Intrinsically Disordered Proteins

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In the last 2 decades it has become increasingly evident that a large number of proteins are either fully or partially disordered. Intrinsically disordered proteins lack a stable 3D structure, are ubiquitous and fulfill essential biological functions. Their conformational heterogeneity is encoded in their amino acid sequences, thereby allowing intrinsically disordered proteins or regions to be recognized based on properties of these sequences. The identification of disordered regions facilitates the functional annotation of proteins and is instrumental for delineating boundaries of protein domains amenable to structural determination with X-ray crystallization. This article discusses a comprehensive selection of databases and methods currently employed to disseminate experimental and putative annotations of disorder, predict disorder and identify regions involved in induced folding. It also provides a set of detailed instructions that should be followed to perform computational analysis of disorder.KEYWORDS disorder databases and metaservers; induced folding; intrinsic disorder; intrinsically disordered proteins; intrinsically disordered regions; prediction methods

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“…Indeed, although globular proteins contribute most of their hydrophobic residues to the protein core, IDPs expose their few hydrophobic residues to the surface, thereby allowing interaction with binding partners. As a result, IDP interfaces make more hydrophobic contacts (33% for IDPs and 22% for ordered proteins), whereas ordered interfaces make more polar interactions (122). A notable exception is provided by the SeV N TAIL -P XD complex that mainly relies on polar contacts and is therefore impaired by high salt concentrations (83).…”

Section: Structural Models Of Henipavirus N Tail -P Xd Complexes and mentioning

confidence: 99%

Characterization of the Interactions between the Nucleoprotein and the Phosphoprotein of Henipavirus

Habchi

Blangy

Mamelli

et al. 2011

Journal of Biological Chemistry

165

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The Henipavirus genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid that recruits the polymerase complex via the phosphoprotein (P). In a previous study, we reported that in henipaviruses, the N-terminal domain of the phosphoprotein and the C-terminal domain of the nucleoprotein (N TAIL ) are both intrinsically disordered. Here we show that Henipavirus N TAIL domains are also disordered in the context of full-length nucleoproteins. We also report the cloning, purification, and characterization of the C-terminal X domains (P XD ) of Henipavirus phosphoproteins. Using isothermal titration calorimetry, we show that N TAIL and P XD form a 1:1 stoichiometric complex that is stable under NaCl concentrations as high as 1 M and has a K D in the M range. Using far-UV circular dichroism and nuclear magnetic resonance, we show that P XD triggers an increase in the ␣-helical content of N TAIL . Using fluorescence spectroscopy, we show that P XD has no impact on the chemical environment of a Trp residue introduced at position 527 of the Henipavirus N TAIL domain, thus arguing for the lack of stable contacts between the C termini of N TAIL and P XD . Finally, we present a tentative structural model of the N TAIL -P XD interaction in which a short, order-prone region of N TAIL (␣-MoRE; amino acids 473-493) adopts an ␣-helical conformation and is embedded between helices ␣2 and ␣3 of P XD , leading to a relatively small interface dominated by hydrophobic contacts. The present results provide the first detailed experimental characterization of the N-P interaction in henipaviruses and designate the N TAIL -P XD interaction as a valuable target for rational antiviral approaches.

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Molecular Principles of the Interactions of Disordered Proteins

Cited by 250 publications

References 55 publications

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

How disordered is my protein and what is its disorder for? A guide through the “dark side” of the protein universe

Characterization of the Interactions between the Nucleoprotein and the Phosphoprotein of Henipavirus

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