A5062181294- Heat shock proteins research
- Protein Structure and Dynamics
- Enzyme Structure and Function
- Toxin Mechanisms and Immunotoxins
- RNA and protein synthesis mechanisms
- ZnO doping and properties
- Computational Drug Discovery Methods
- Ga2O3 and related materials
- Quantum Dots Synthesis And Properties
- Viral Infectious Diseases and Gene Expression in Insects
- Thermal Regulation in Medicine
- Endoplasmic Reticulum Stress and Disease
- Photosynthetic Processes and Mechanisms
- Plant and Biological Electrophysiology Studies
- Cellular Mechanics and Interactions
- Optimism, Hope, and Well-being
- Plant biochemistry and biosynthesis
- Neurobiology and Insect Physiology Research
- Photoreceptor and optogenetics research
- Hemoglobin structure and function
École Polytechnique Fédérale de Lausanne
2024
University of Lausanne
2019-2023
Indian Institute of Technology Hyderabad
2023
Institute of Genomics and Integrative Biology
2012-2022
Academy of Scientific and Innovative Research
2015-2021
Leaf-feeding insects trigger high-amplitude, defense-inducing electrical signals called slow wave potentials (SWPs). These are thought to be triggered by the long-distance transport of low molecular mass elicitors termed Ricca's factors. We sought mediators leaf-to-leaf signaling in Arabidopsis thaliana and identified them as β-THIOGLUCOSIDE GLUCOHYDROLASE 1 2 (TGG1 TGG2). SWP propagation from insect feeding sites was strongly attenuated tgg1 tgg2 mutants wound-response cytosolic Ca2+...
Abstract Detailed understanding of the mechanism by which Hsp70 chaperones protect cells against protein aggregation is hampered lack a comprehensive characterization aggregates, are typically heterogeneous. Here we designed reporter chaperone substrate, MLucV, composed stress-labile luciferase flanked stress-resistant fluorescent domains, upon denaturation formed discrete population small aggregates. Combining Förster resonance energy transfer and enzymatic activity measurements provided...
The role of bacterial DnaJ protein as a cochaperone DnaK is strongly appreciated. Although unaccompanied by can bind unfolded well native substrate proteins, its an individual chaperone remains elusive. In this study, we demonstrate that binds model non-native with low nanomolar dissociation constant and, more importantly, modulates the structure state. structural modulation achieved different compared to DnaK–DnaJ complex. nature exerted suggestive unique unfolding activity on chaperone....
Many proteins comprising of complex topologies require molecular chaperones to achieve their unique three-dimensional folded structure. The E.coli chaperone, GroEL binds with a large number unfolded and partially proteins, facilitate proper folding prevent misfolding aggregation. Although the major structural components are well defined, scaffolds non-native substrates that determine chaperone-mediated have been difficult recognize. Here we performed all-atomistic replica-exchange dynamics...
In eukaryotes, Hsp110s are unambiguous cognates of the Hsp70 chaperones, in primary sequence, domain organization, and structure. function as nucleotide exchange factors (NEFs) for Hsp70s although their apparent loss Hsp70-like chaperone activity, nature interdomain communication, breadth functions still puzzling. Here, by combining single-molecule FRET, small angle X-ray scattering measurements (SAXS), MD simulation, we show that yeast Hsp110, Sse1 lacks canonical allostery. However,...
The Hsp70 chaperones control protein homeostasis in all ATP-containing cellular compartments. J-domain proteins (JDPs) co-evolved with Hsp70s to trigger ATP-hydrolysis and catalytically upload various substrate polypeptides need be structurally modified by the chaperone. Here, we measured disaggregation refolding activities of main yeast cytosolic Hsp70, Ssa1, presence its most abundant JDPs, Sis1 Ydj1, two swap mutants, which J-domains have been interchanged. observed differences four...
Significance Hsp60/10 chaperonins are critical for cellular proteostasis in all kingdoms of life. In this study, we present that across different species have differences the cavity properties and correlatively their capability to remove entropic traps folding pathways GroEL/ES substrates; is affected majorly by negative-charge density inside chaperonin cavity. This dissimilarity leads a remarkable difference between homologs buffering mutational variations. However, most them can nonnative...
Partially charged chiral molecules act as spin filters, with preference for electron transport toward one type of ("up" or "down"), depending on their handedness. This effect is named the induced selectivity (CISS) effect. A consequence this phenomenon polarization concomitant electric in molecules. These findings were shown by adsorbing magnetic surfaces and investigating spin-exchange interaction between surface molecule. field study was developed using artificial Here we used such to...
Abstract The Hsp70 chaperones control protein homeostasis in all ATP-containing cellular compartments. J-domain proteins (JDPs) co-evolved with Hsp70s to trigger ATP-hydrolysis and catalytically upload various substrate polypeptides need be structurally modified by the chaperone. Here, we measured disaggregation refolding activities of main yeast cytosolic Hsp70, Ssa1, presence its most abundant JDPs, Sis1 Ydj1, two swap mutants, which J-domains have been interchanged. observed differences...
Abstract A detailed understanding of the mechanism by which Hsp70 chaperones protect cells against protein aggregation is hampered characterization aggregates, are typically heterogeneous. To tackle this problem, we designed here a reporter chaperone substrate, MLucV, composed stress-labile luciferase core, flanked stress-resistant fluorescent mTFP and Venus domains, upon denaturation formed discrete stable population small aggregates. Combining Förster Resonance Energy Transfer enzymatic...
ABSTRACT The folding landscape of proteins can change during evolution with the accumulation mutations that may introduce entropic or enthalpic barriers in protein pathway, making it a possible substrate molecular chaperones vivo . Can nature such physical dictate feasibility chaperone-assistance? To address this, we have simulated evolutionary step to chaperone-dependence keeping GroEL/ES as target chaperone and GFP model an unbiased screen. We find mutation conferring dependence vitro...
Understanding the folding pathway of any protein is utmost importance for deciphering problems under adverse conditions. We can obtain important information about by monitoring from its unfolded state. It usually very difficult to monitor process in real time as generally fast, and we need a suitable read out. In this protocol, have solved issue using that non-fluorescent state but fluoresces native after folding. The kinetics refolding be monitored following increase fluorescence time....