Browse
Submit Data
Databases
API
Help

Dataset Information

21 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Ultrastable cellulosome-adhesion complex tightens under load.

ABSTRACT: Challenging environments have guided nature in the development of ultrastable protein complexes. Specialized bacteria produce discrete multi-component protein networks called cellulosomes to effectively digest lignocellulosic biomass. While network assembly is enabled by protein interactions with commonplace affinities, we show that certain cellulosomal ligand-receptor interactions exhibit extreme resistance to applied force. Here, we characterize the ligand-receptor complex responsible for substrate anchoring in the Ruminococcus flavefaciens cellulosome using single-molecule force spectroscopy and steered molecular dynamics simulations. The complex withstands forces of 600-750 pN, making it one of the strongest bimolecular interactions reported, equivalent to half the mechanical strength of a covalent bond. Our findings demonstrate force activation and inter-domain stabilization of the complex, and suggest that certain network components serve as mechanical effectors for maintaining network integrity. This detailed understanding of cellulosomal network components may help in the development of biocatalysts for production of fuels and chemicals from renewable plant-derived biomass.

SUBMITTER: Schoeler C

PROVIDER: S-EPMC4266597 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

All-in-one flexible supercapacitor with ultrastable performance under extreme load.

Project description:Fiber-type solid-state supercapacitors are being widely investigated as stable power supply for next-generation wearable and flexible electronics. Integrating both high charge storage capability and superior mechanical properties into one fiber is crucial to realize fiber-type solid-state supercapacitors. In this study, we design a “jeweled necklace”–like hybrid composite fiber comprising double-walled carbon nanotube yarn and metal-organic frameworks (MOFs). Subsequent heat treatment transforms MOFs into MOF-derived carbon (MDC), thereby maximizing energy storage capability while retaining the superior mechanical properties. The hybrid fibers with tunable properties, including thickness and MDC loading amount, exhibit a high energy density of 7.54 milliwatt-hour per cubic centimeter at a power density of 190.94 milliwatt per cubic centimeter. The mechanical robustness of the hybrid fibers allows them to operate under various mechanical deformation conditions. Furthermore, it is demonstrated that the resulting superstrong fiber delivers sufficient power to switch on light-emitting diodes by itself while suspending 10-kilogram weight.

| S-EPMC8730631 | biostudies-literature

Direction Matters: Monovalent Streptavidin/Biotin Complex under Load.

Project description:Novel site-specific attachment strategies combined with improvements of computational resources enable new insights into the mechanics of the monovalent biotin/streptavidin complex under load and forced us to rethink the diversity of rupture forces reported in the literature. We discovered that the mechanical stability of this complex depends strongly on the geometry in which force is applied. By atomic force microscopy-based single molecule force spectroscopy we found unbinding of biotin to occur beyond 400 pN at force loading rates of 10 nN/s when monovalent streptavidin was tethered at its C-terminus. This value is about twice as high than that for N-terminal attachment. Steered molecular dynamics simulations provided a detailed picture of the mechanics of the unbinding process in the corresponding force loading geometries. Using machine learning techniques, we connected findings from hundreds of simulations to the experimental results, identifying different force propagation pathways. Interestingly, we observed that depending on force loading geometry, partial unfolding of N-terminal region of monovalent streptavidin occurs before biotin is released from the binding pocket.

| S-EPMC6486461 | biostudies-literature

Crocus sativus Extract Tightens the Blood-Brain Barrier, Reduces Amyloid β Load and Related Toxicity in 5XFAD Mice.

Project description:Crocus sativus, commonly known as saffron or Kesar, is used in Ayurveda and other folk medicines for various purposes as an aphrodisiac, antispasmodic, and expectorant. Previous evidence suggested that Crocus sativus is linked to improving cognitive function in Alzheimer's disease (AD) patients. The aim of this study was to in vitro and in vivo investigate the mechanism(s) by which Crocus sativus exerts its positive effect against AD. The effect of Crocus sativus extract on Aβ load and related toxicity was evaluated. In vitro results showed that Crocus sativus extract increases the tightness of a cell-based blood-brain barrier (BBB) model and enhances transport of Aβ. Further in vivo studies confirmed the effect of Crocus sativus extract (50 mg/kg/day, added to mice diet) on the BBB tightness and function that was associated with reduced Aβ load and related pathological changes in 5XFAD mice used as an AD model. Reduced Aβ load could be explained, at least in part, by Crocus sativus extract effect to enhance Aβ clearance pathways including BBB clearance, enzymatic degradation and ApoE clearance pathway. Furthermore, Crocus sativus extract upregulated synaptic proteins and reduced neuroinflammation associated with Aβ pathology in the brains of 5XFAD mice. Crocin, a major active constituent of Crocus sativus and known for its antioxidant and anti-inflammatory effect, was also tested separately in vivo in 5XFAD mice. Crocin (10 mg/kg/day) was able to reduce Aβ load but to a lesser extent when compared to Crocus sativus extract. Collectively, findings from this study support the positive effect of Crocus sativus against AD by reducing Aβ pathological manifestations.

| S-EPMC5559303 | biostudies-literature

Modeling the self-assembly of the cellulosome enzyme complex.

Project description:Most bacteria use free enzymes to degrade plant cell walls in nature. However, some bacteria have adopted a different strategy wherein enzymes can either be free or tethered on a protein scaffold forming a complex called a cellulosome. The study of the structure and mechanism of these large macromolecular complexes is an active and ongoing research topic, with the goal of finding ways to improve biomass conversion using cellulosomes. Several mechanisms involved in cellulosome formation remain unknown, including how cellulosomal enzymes assemble on the scaffoldin and what governs the population of cellulosomes created during self-assembly. Here, we present a coarse-grained model to study the self-assembly of cellulosomes. The model captures most of the physical characteristics of three cellulosomal enzymes (Cel5B, CelS, and CbhA) and the scaffoldin (CipA) from Clostridium thermocellum. The protein structures are represented by beads connected by restraints to mimic the flexibility and shapes of these proteins. From a large simulation set, the assembly of cellulosomal enzyme complexes is shown to be dominated by their shape and modularity. The multimodular enzyme, CbhA, binds statistically more frequently to the scaffoldin than CelS or Cel5B. The enhanced binding is attributed to the flexible nature and multimodularity of this enzyme, providing a longer residence time around the scaffoldin. The characterization of the factors influencing the cellulosome assembly process may enable new strategies to create designers cellulosomes.

| S-EPMC3037675 | biostudies-literature

Ultrastable Au nanoparticles on titania through an encapsulation strategy under oxidative atmosphere.

Project description:Supported gold catalysts play a crucial role in the chemical industry; however, their poor on-stream stability because of the sintering of the gold nanoparticles restricts their practical application. The strong metal-support interaction (SMSI), an important concept in heterogeneous catalysis, may be applied to construct the structure of catalysts and, hence, improve their reactivity and stability. Here we report an ultrastable Au nanocatalyst after calcination at 800 °C, in which Au nanoparticles are encapsulated by a permeable TiOx thin layer induced by melamine under oxidative atmosphere. Owning to the formed TiOx overlayer, the resulting Au catalyst is resistant to sintering and exhibits excellent activity and stability for catalytic CO oxidation. Furthermore, this special strategy can be extended to colloidal Au nanoparticles supported on TiO2 and commercial gold catalyst denoted as RR2Ti, providing a universal way to engineer and develop highly stable supported Au catalysts with tunable activity.

| S-EPMC6923380 | biostudies-literature

Cell adhesion. The minimal cadherin-catenin complex binds to actin filaments under force.

Project description:Linkage between the adherens junction (AJ) and the actin cytoskeleton is required for tissue development and homeostasis. In vivo findings indicated that the AJ proteins E-cadherin, ?-catenin, and the filamentous (F)-actin binding protein ?E-catenin form a minimal cadherin-catenin complex that binds directly to F-actin. Biochemical studies challenged this model because the purified cadherin-catenin complex does not bind F-actin in solution. Here, we reconciled this difference. Using an optical trap-based assay, we showed that the minimal cadherin-catenin complex formed stable bonds with an actin filament under force. Bond dissociation kinetics can be explained by a catch-bond model in which force shifts the bond from a weakly to a strongly bound state. These results may explain how the cadherin-catenin complex transduces mechanical forces at cell-cell junctions.

| S-EPMC4364042 | biostudies-literature

Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex.

Project description:The utilization of organized supramolecular assemblies to exploit the synergistic interactions afforded by close proximity, both for enzymatic synthesis and for the degradation of recalcitrant substrates, is an emerging theme in cellular biology. Anaerobic bacteria harness a multiprotein complex, termed the "cellulosome," for efficient degradation of the plant cell wall. This megadalton catalytic machine organizes an enzymatic consortium on a multifaceted molecular scaffold whose "cohesin" domains interact with corresponding "dockerin" domains of the enzymes. Here we report the structure of the cohesin-dockerin complex from Clostridium thermocellum at 2.2-A resolution. The data show that the beta-sheet cohesin domain interacts predominantly with one of the helices of the dockerin. Whereas the structure of the cohesin remains essentially unchanged, the loop-helix-helix-loop-helix motif of the dockerin undergoes conformational change and ordering compared with its solution structure, although the classical 12-residue EF-hand coordination to two calcium ions is maintained. Significantly, internal sequence duplication within the dockerin is manifested in near-perfect internal twofold symmetry, suggesting that both "halves" of the dockerin may interact with cohesins in a similar manner, thus providing a higher level of structure to the cellulosome and possibly explaining the presence of "polycellulosomes." The structure provides an explanation for the lack of cross-species recognition between cohesin-dockerin pairs and thus provides a blueprint for the rational design, construction, and exploitation of these catalytic assemblies.

| S-EPMC283503 | biostudies-literature

PCNA tightens its hold on the nucleus.

Project description: Not available

| S-EPMC4613660 | biostudies-literature

Actin network growth under load.

Project description:Many processes in eukaryotic cells, including the crawling motion of the whole cell, rely on the growth of branched actin networks from surfaces. In addition to their well-known role in generating propulsive forces, actin networks can also sustain substantial pulling loads thanks to their persistent attachment to the surface from which they grow. The simultaneous network elongation and surface attachment inevitably generate a force that opposes network growth. Here, we study the local dynamics of a growing actin network, accounting for simultaneous network elongation and surface attachment, and show that there exist several dynamical regimes that depend on both network elasticity and the kinetic parameters of actin polymerization. We characterize this in terms of a phase diagram and provide a connection between mesoscopic theories and the microscopic dynamics of an actin network at a surface. Our framework predicts the onset of instabilities that lead to the local detachment of the network and translate to oscillatory behavior and waves, as observed in many cellular phenomena and in vitro systems involving actin network growth, such as the saltatory dynamics of actin-propelled oil drops.

| S-EPMC3296029 | biostudies-literature

Enhanced microbial utilization of recalcitrant cellulose by an ex vivo cellulosome-microbe complex.

Project description:A cellulosome-microbe complex was assembled ex vivo on the surface of Bacillus subtilis displaying a miniscaffoldin that can bind with three dockerin-containing cellulase components: the endoglucanase Cel5, the processive endoglucanase Cel9, and the cellobiohydrolase Cel48. The hydrolysis performances of the synthetic cellulosome bound to living cells, the synthetic cellulosome, a noncomplexed cellulase mixture with the same catalytic components, and a commercial fungal enzyme mixture were investigated on low-accessibility recalcitrant Avicel and high-accessibility regenerated amorphous cellulose (RAC). The cell-bound cellulosome exhibited 4.5- and 2.3-fold-higher hydrolysis ability than cell-free cellulosome on Avicel and RAC, respectively. The cellulosome-microbe synergy was not completely explained by the removal of hydrolysis products from the bulk fermentation broth by free-living cells and appeared to be due to substrate channeling of long-chain hydrolysis products assimilated by the adjacent cells located in the boundary layer. Our results implied that long-chain hydrolysis products in the boundary layer may inhibit cellulosome activity to a greater extent than the short-chain products in bulk phase. The findings that cell-bound cellulosome expedited the microbial cellulose utilization rate by 2.3- to 4.5-fold would help in the development of better consolidated bioprocessing microorganisms (e.g., B. subtilis) that can hydrolyze recalcitrant cellulose rapidly at low secretory cellulase levels.

| S-EPMC3294486 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data