Publications by authors named "Tatiana Stanishneva-Konovalova"
Variants of SARS-CoV-2 keep emerging and causing new waves of COVID-19 around the world. Effective new approaches in drug development are based on the binding of agents, such as neutralizing monoclonal antibodies to a receptor-binding domain (RBD) of SARS-CoV-2 spike protein. However, mutations in RBD may lower the affinity of previously developed antibodies.
View Article and Find Full Text PDFChaperonins, a family of molecular chaperones, assist protein folding in all domains of life. They are classified into two groups: bacterial variants and those present in endosymbiotic organelles of eukaryotes belong to group I, while group II includes chaperonins from the cytosol of archaea and eukaryotes. Recently, chaperonins of a prospective new group were discovered in giant bacteriophages; however, structures have been determined for only two of them.
View Article and Find Full Text PDFThe molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrP, could lead to pathogenic transformation of the latter to the aggregation-prone PrP form. Here, the molecular basis of the interactions in the GroEL-PrP complex is studied with cryo-EM and molecular dynamics approaches.
View Article and Find Full Text PDFThe GroEL-GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release. Structural methods helped to reveal several conformational states and provide more information about the chaperonin functional cycle.
View Article and Find Full Text PDFArticle Synopsis
- Chaperonins are essential protein complexes that help proteins fold correctly and prevent aggregation, operating in an ATP-dependent manner.
- They are categorized into two main groups: group I (found in bacteria, mitochondria, and chloroplasts) and group II (found in archaea and eukaryotic cytoplasm), while newly found viral chaperonins are not included in these categories.
- The study detailed the structures of a single-ring chaperonin from a bacteriophage, revealing unique arrangements of subunits that respond differently to nucleotide binding, suggesting this chaperonin represents a potential new classification group.
Bin/Amphyphysin/Rvs (BAR) domain proteins form a key link between membrane remodeling and cytoskeleton dynamics. They are dimers that bind to membranes via electrostatic interactions with different preferences toward negatively charged lipids. In the present article, we examine the interactions of the F-BAR domain of nervous wreck (Nwk) with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P )-containing membranes using coarse-grained molecular dynamics.
View Article and Find Full Text PDFFormins are essential actin assembly factors whose activities are controlled by a diverse array of binding partners. Until now, most formin ligands have been studied on an individual basis, leaving open the question of how multiple inputs are integrated to regulate formins in vivo. Here, we show that the F-BAR domain of Hof1 interacts with the FH2 domain of the formin Bnr1 and blocks actin nucleation.
View Article and Find Full Text PDFArticle Synopsis
- Autoinhibitory interactions between the SH3 and F-BAR domains of F-BAR proteins regulate membrane remodeling, but the structural basis of this autoregulation and its effect on cellular interactions are not well understood.
- The study utilized single-particle electron microscopy to analyze the F-BAR protein Nervous Wreck (Nwk) in soluble and membrane-bound forms, revealing that the SH3 domains reposition rather than fully detach upon membrane binding.
- Findings indicate that Nwk's autoregulation limits the activity of SH3 domains in actin filament assembly and affects synaptic growth and organization in Drosophila neurons, suggesting a coordinated relationship between membrane interactions and SH3 domain functions.
Article Synopsis
- Eukaryotic cells rely on F-BAR domain proteins, which are capable of bending membranes for shaping cellular compartments, but their varying membrane-deforming activities are not fully understood.
- The Nwk protein's F-BAR domain forms a unique zigzag structure that enhances its ability to create distinct membrane shapes, differing from other F-BAR proteins.
- This study reveals how structural features of the Nwk F-BAR domain contribute to its membrane sculpting abilities, highlighting a new aspect of how F-BAR proteins can induce various membrane curvatures.