bioRxiv Science⌕ Search

bioRxiv · 10.1101/2020.02.05.935551

Direct label-free imaging of nanodomains in biomimetic and biological membranes by cryogenic electron microscopy

Abstract

The nanoscale organization of biological membranes into structurally and compositionally distinct lateral domains is believed to be central to membrane function. The nature of this organization has remained elusive due to a lack of methods to directly probe nanoscopic membrane features. We show here that cryogenic electron microscopy (cryoEM) can be used to directly image coexisting nanoscopic domains in synthetic and bio-derived membranes without extrinsic probes. Analyzing a series of single-component liposomes composed of synthetic lipids of varying lengths, we demonstrate that cryoEM can distinguish bilayer thickness differences as small as 0.5 [A], comparable to the resolution of small-angle scattering methods. Simulated images from computational models reveal that features in cryoEM images result from a complex interplay between the atomic distribution normal to the plane of the bilayer and imaging parameters. Simulations of phase separated bilayers were used to predict two sources of contrast between coexisting ordered and disordered phases within a single liposome, namely differences in membrane thickness and molecular density. We observe both sources of contrast in biomimetic membranes composed of saturated lipids, unsaturated lipids, and cholesterol. When extended to isolated mammalian plasma membranes, these methods reveal similar nanoscale lateral heterogeneities. The methods reported here for direct, probe-free imaging of nanodomains in unperturbed membranes open new avenues for investigation of nanoscopic membrane organization. SIGNIFICANCEWe have used cryoEM to achieve direct, probe-free imaging of lateral domains in biomimetic lipid membranes under native conditions and to characterize differences in their structures. First, measurements of membrane thickness in laterally uniform single-component membranes show that cryoEM is capable of sub-angstrom resolution of interleaflet membrane thickness. All-atom simulations are used to predict the cryo-EM appearance of submicron domains in vesicles with coexisting liquid domains and these are quantitatively validated by direct imaging of phase separated membranes. We then extend this approach to observe nanoscopic domains in isolated cellular membranes, comprising the first direct imaging of nanodomains in biomembranes.

Source connections

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Heberle, F. A., Doktorova, M., Scott, H. L., Skinkle, A. D., Waxham, N., Levental, I.. 2020-02-05. Direct label-free imaging of nanodomains in biomimetic and biological membranes by cryogenic electron microscopy. https://doi.org/10.1101/2020.02.05.935551

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Expression-System Biases Compromise the Functional Assessment of KCNH2 Variants and Clinical Risk Assessment

Background: Functional characterization of KCNH2 variants is essential for assessing pathogenicity in long QT syndrome type 2. Because hERG channels assemble as tetramers, the relative expression of wild-type (WT) and variant subunits critically influences channel function and pathogenicity assessment. However, commonly used experimental systems may not reproduce the balanced allelic expression observed in heterozygous patients. Methods: Allele-specific KCNH2 expression was analyzed in two independent RNA-sequencing datasets from human left ventricular tissue. Using the dominant-negative T74R hERG variant as a model, we calibrated the relationship between WT-to-variant expression ratios and hERG current amplitude. Using automated patch-clamp electrophysiology, we compared 3 dual-expression strategies: internal ribosome entry site (IRES), P2A-linked tandem constructs, and dual cytomegalovirus promoter (dCMV) constructs. Co-electroporation of WT and variant plasmids in different ratios was the reference. Results: Allele-specific expression analysis supported balanced KCNH2 expression in human left ventricular tissue. At a 1:1 WT-to-T74R expression ratio, hERG current amplitude was reduced to 31.0% of WT, consistent with a dominant-negative mechanism in which incorporation of 2 or more T74R subunits renders the channel nonfunctional. All 3 dual-expression strategies produced substantial expression imbalances, with the first cassette consistently favored. IRES constructs showed the greatest asymmetry. P2A constructs partially improved expression balance but introduced an additional N-terminal proline in the second cassette altering T74R-associated trafficking and channel biophysics. The dCMV system also failed to achieve balanced expression, including after stable integration. Co-electroporation of separate WT and variant plasmids provided the most reliable means of controlling their relative expression. Conclusions: Commonly used dual-expression constructs do not reliably reproduce balanced WT and variant hERG expression, potentially distorting assessments of dominant-negative effects and variant pathogenicity. Co-electroporation of separate plasmids provides a robust approach for high-throughput functional phenotyping under heterozygous conditions, with implications for the interpretation of KCNH2 variants and potentially other genes encoding multimeric ion channels.

biophysics↗

Learning from Hi-C reveals nuclear dynamical reorganization in budding yeast across the cell cycle

Hi-C contact maps provide population-averaged measurements of chromosomal contacts. Converting these measurements, however, into three-dimensional structures and associated dynamics remains an underdetermined problem. Existing approaches broadly fall into two classes. Data-driven reconstruction methods that infer either a consensus structure or an ensemble of conformations, but do not inform on chromosome dynamics. Physics-based models, which generate dynamical trajectories, but require prior assumptions about nuclear geometry, chromatin mechanics, tethering, or molecular interactions. Here, we bridge these approaches using the Full-Inversion Chromatin model, a data-driven whole-genome polymer framework that learns an effective force field directly from Hi-C contact probabilities, integrated with Serpentine, a tool to quantify contact-map discrepancies while accounting for differences in sequencing coverage and sparsity. This generates structural ensembles of chromosomes and effective chromatin dynamics. We apply this method at 5-kb resolution to Saccharomyces cerevisiae in G1, mid-S, S/G2, G2/M, anaphase, and quiescence. Without explicitly imposing the spindle pole body, centromere or telomere tethering, predefined chromatin states, or nuclear-envelope interactions, the inferred ensembles recover these major features of yeast nuclear organization. Importantly, although dynamical information is not used during model training, the resulting polymer trajectories reproduce the subdiffusive scaling and chromosomal variations of independently measured chromatin motion. The model further predicts heterogeneous mobility along chromosomes and a distinctive telomere-dependent dynamical organization. Thus, population-averaged Hi-C contacts contain sufficient information to infer not only three-dimensional genome organization, but also effective, locus-dependent chromatin dynamics.

biophysics↗

One high-order ion-coupling mechanism generates multiple SLC1A stoichiometries

Human excitatory amino acid transporter 2 (hEAAT2) is a glial transporter that clears glutamate and aspartate from the extracellular space to terminate neurotransmission. When this essential role is disrupted, excess extracellular glutamate causes excitotoxicity and neurological disease. hEAAT2 transports amino acids into cells against their concentration gradients by coupling uptake to the co-transport of Na+ and H+, and counter-transport of K+. Substrate transport also activates a thermodynamically uncoupled Cl- conductance, whose significance is unknown. Here, to dissect the molecular mechanisms underlying coupled and uncoupled ion transport by EAATs, we leverage the tractable Drosophila melanogaster homologue dEAAT2, which transports taurine as well as glutamate and aspartate. By functionally characterising dEAAT2, we confirmed it has features of a canonical EAAT transport cycle, including an uncoupled Cl- conductance. However, it functions an ion-independent electroneutral exchanger, in stark contrast to its ion-coupled electrogenic human counterpart. Cryo-electron microscopy (cryo-EM) and computational simulations confirmed the inability of dEAAT2 to transport cations, but just two point mutations conferred Na+, H+, and K+ dependence, reconstituting the complex ion coupling profile of human transporters in the Drosophila exchanger. We also showed that dEAAT2 transports taurine in a complex with Cl-, bestowing a unique Cl--dependence on taurine transport, independent of uncoupled Cl- flux. Our findings show that ancestral exchangers in the EAAT family preserve the machinery to achieve complex ion-coupled transport, revealing the molecular basis of high-order ion coupling in hEAATs.

biophysics↗