Method Article

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

DOI:

10.3791/63057

September 23rd, 2021

In This Article

Summary

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A protocol for the application of paramagnetic relaxation enhancement NMR spectroscopy to detect weak and transient inter- and intra-molecular interactions in intrinsically disordered proteins is presented.

Abstract

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Intrinsically disordered proteins and intrinsically disordered regions within proteins make up a large and functionally significant part of the human proteome. The highly flexible nature of these sequences allows them to form weak, long-range, and transient interactions with diverse biomolecular partners. Specific yet low-affinity interactions promote promiscuous binding and enable a single intrinsically disordered segment to interact with a multitude of target sites. Because of the transient nature of these interactions, they can be difficult to characterize by structural biology methods that rely on proteins to form a single, predominant conformation. Paramagnetic relaxation enhancement NMR is a useful tool for identifying and defining the structural underpinning of weak and transient interactions. A detailed protocol for using paramagnetic relaxation enhancement to characterize the lowly-populated encounter complexes that form between intrinsically disordered proteins and their protein, nucleic acid, or other biomolecular partners is described.

Introduction

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Intrinsic disorder (ID) describes proteins (IDPs) or regions within proteins (IDRs) that do not spontaneously fold into stable secondary or tertiary structures but are biologically active. Generally, the function of IDP/IDRs is to facilitate specific yet reversible interactions with biomolecules at physiological conditions1. Thus, IDPs and IDRs are involved in a range of cellular functions, including recruitment, organization, and stabilization of multi-protein complexes, for example, the assembly and activity of the spliceosome2, recruitment and organization of components at sites of DNA damage3,....

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Protocol

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General requirements for the protocol: protein purification facilities, UV-Vis spectrometer, high-field NMR spectrometer and operating software, post-processing analysis software including; NMRPipe32, Sparky33, (or CCPN Analysis34, or NMRViewJ35).

1. Recombinant expression and purification of a protein for PRE measurements

  1. Design an expression construct for the protein of interest so that there is a single cysteine residue present. Multiple mutations will be required to introduce a free cysteine at different positions in the protein o....

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Results

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Intramolecular 1HN-Γ2 PREs were recorded on a self-associating, intrinsically disordered fragment (residues 171-264) derived from the low-complexity domain of the RNA-binding protein EWSR142 (Figure 3). Residues in close sequential proximity to the spin-label attachment point (e.g., residue 178 or 260 in Figure 3) are expected to be significantly broadened and are not detectable in the spectrum. R.......

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Discussion

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A method for characterizing transient interactions that exist at low populations between intrinsically disordered proteins and various binding partners using PRE has been presented. In the example shown, the protein is self-associating, and thus the PRE may arise from a combination of inter and intramolecular interactions. This method is readily extended to heterogeneous samples where the interactions between two different proteins may be characterized. Complementary information about how different regions of the protein.......

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Disclosures

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All authors have read and approved the manuscript. No conflicts of interest are declared.

Acknowledgements

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We thank Drs. Jinfa Ying and Kristin Cano for helpful discussions and technical assistance. DSL is a St. Baldrick's Scholar and acknowledges the support of the St. Baldrick's Foundation (634706). This work was supported in part by the Welch Foundation (AQ-2001-20190330) to DSL, the Max and Minnie Tomerlin Voelcker Fund (Voelcker Foundation Young Investigator Grant to DSL), UTHSA Start-Up Funds to DSL, and a Greehey Graduate Fellowship in Children's Health to CNJ. This work is based upon research conducted in the Structural Biology Core Facilities, part of the Institutional Research Cores at the University of Texas Health Science Center at San Antonio suppo....

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Materials

List of materials used in this article
NameCompanyCatalog NumberComments
0.45 µm and 0.22 µm syringe filtersMillipore SigmaSLHVM33RS
SLGVR33RS
Filter lysate before first purification step and before size exclusion chromatography.
100 mm Petri DishFisherFB0875713Agar plates for bacterial transformation.
14N Ammonium chlorideSigma Aldrich576794Use of 15N in M9 medium will produce an NMR visible protein, 14N will produces an NMR invisible protein
15N Ammonium chlorideSigma Aldrich299251Use of 15N in M9 medium will produce an NMR visible protein, 14N will produces an NMR invisible protein
3 L Fernbach baffled flaskCorning431523Bacterial expression culture
3-Maleimido-ProxylSigma Aldrich253375Nitroxide spin label
50 mL conical centrifuge tubesThermo Fisher14-432-22Solution/protein storage
Amicon centrifugal filterMillipore SigmaUFC900308Protein concentration
AmpicillanSigma AldrichA5354Antibiotic for a selective marker, exact choice depends on the expression construct plasmid
Analytical balanceOahus30061978Explorer Pro, for weighing reagents
Ascorbic acidSigma AldrichAX1775Reduces nitroxide spin label
AutoclaveSterilize glassware and culture media
Calcium chlorideSigma AldrichC4901M9 media component
Centrifuge bottlesThermo Fisher010-1459Harvest E. coli cells after recombinant protein expression
Centrifuge, hand-crankThomas Scientific0241C68Boekel hand-driven, low-speed centrifuge with 15 mL buckets that can accommodate NMR tubes
Chelex 100Sigma AldrichC7901Remove contaminating paramagnetic compounds from buffer solutions
Computer workstationLinux or Mac OS compatable with NMR data processing and analysis software packages such as NMRPipe and Sparky
Deuterium oxideSigma Aldrich151882Needed for NMR lock signal
DextroseSigma AldrichD9434M9 media component
Dibasic Sodium PhosphateSigma AldrichS5136M9 media component
Ellman's reagent (5,5-dithio-bis-(2-nitrobenzoic acid)Thermo Fisher22582Quantification of free cystiene residues
High speed centrifuge tubesThermo Fisher3114-0050Used to clear bacterial lysate.
High-field NMR instrument (600 - 800 MHz)BrukerEquiped with a multichannel cryogenic probe and temperature control
IMAC column, HisTrap FFCytvia17528601Initial fractionation of crude bacterial lysate
Isopropyl B-D-thiogalactoside (IPTG)Sigma AldrichI6758Induces protein expression for genes under control of lac operator
LB agarThermo Fisher22700025Items are used for transforming E. coli to express protein of interest, substitions for any of these items with like products is acceptable.
LB brothThermo Fisher12780052
Low-pressure chromatography systemBio-Rad7318300BioRad BioLogic is used for low-pressure chomatograph such as running IMAC columns
Magnesium sulfateSigma AldrichM7506M9 media component
Medium pressure chromatography systemBio-Rad7880007BioRad NGC equipped with a multi-wavelength detector, pH and conductivity monitors, and automatic fraction collector
MEM vitamin solutionSigma AldrichM6895M9 media component
MicrofluidizerAvestinEmulsiFlex-C3Provides rapid and efficient bacterial cell lysis
MicropipettesThermo FisherCalibrated set of micropippetters with properly fitting disposable tips (available from multiple manufacturers e.g. Eppendorf)
Monobasic potassium phosphateSigma Aldrich1551139M9 media component
NMR pipettesSigma Aldrich255688To remove sample from NMR tube
NMR sample tubeNewEraNE-SL5Suitable for high-field NMR spectrometers
Preparative CentrifugeBeckman CoulterAvanti J-HCHarvest E. coli cells after recombinant protein expression
Round bottom polystyrene centrifuge tubesCorning352057Clear bacterial lysate
Shaking incubatorEppendorfS44I200005Temperature controlled growth of E. coli starter and expression cultures
Sodium chlorideSigma AldrichS5886M9 media component
Sonicating water bath and vacuum sourceThomas ScientificUsed to degas buffer solutions
SonicatorThermo FisherFB505110Used for bacterial cell lysis or shearing bacterial DNA
SpectrophotometerImplenOD600 DiluphotometerMonitor growth of E.coli protein expression cultures
Superdex 200 16/600 size exculsion columCytvia28989333Final protein purification step
Topspin software, version 3.2 or laterBrukerOperating software for the NMR instrument
Transformation competent E. coli cellsThermo FisherC600003One Shot BL21 Star (DE3) chemically competent E. coli, other strains may be compatable
Tris(2-carboxyethyl)phosphine (TCEP)ThermoFisher20490Reducing agent compatable with some sulfhydryl-reactive conjugations
UV-Vis spectrophotometerImplenNP80Measure protein concentration.
Water bath, temperature controlledThermoFisherFSGPD25For heat shock step of bacterial transformation
Yeast extractSigma AldrichY1625For supplementing M9 media if required

References

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  1. Dyson, H. J., Wright, P. E. Intrinsically unstructured proteins and their functions. Nature Reviews: Molecular Cell Biology. 6 (3), 197-208 (2005).
  2. Korneta, I., Bujnicki, J. M. Intrinsic disorder in the human spliceosomal proteome. PLoS Computational Biology<....

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Tags

Paramagnetic Relaxation EnhancementIntrinsically Disordered ProteinsProtein Self AssociationTransient Protein InteractionsNMR SpectroscopySpin LabelingAmide Proton T2Protein CondensationSize Exclusion ChromatographyDynamic Light Scattering

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