Inari Kursula
University of Bergen, Biomedicine, Faculty Member
Juxtanodin, also called ermin, is an F-actin-binding protein expressed by oligodendrocytes, the myelin-forming cells of the central nervous system. While juxtanodin carries a short conserved F-actin-binding segment at its C terminus, it... more
Juxtanodin, also called ermin, is an F-actin-binding protein expressed by oligodendrocytes, the myelin-forming cells of the central nervous system. While juxtanodin carries a short conserved F-actin-binding segment at its C terminus, it otherwise shares no similarity with known protein sequences. We carried out a structural characterization of recombinant juxtanodin in solution. Juxtanodin turned out to be intrinsically disordered, as evidenced by conventional and synchrotron radiation CD spectroscopy. Small-angle X-ray scattering indicated that juxtanodin is a monomeric, highly elongated, unfolded molecule. Ensemble optimization analysis of the data suggested also the presence of more compact forms of juxtanodin. The C terminus was a strict requirement for co-sedimentation of juxtanodin with microfilaments, but juxtanodin had only mild effects on actin polymerization. The disordered nature of juxtanodin may predict functions as a protein interaction hub, although F-actin is its onl...
Research Interests:
Research Interests:
Research Interests:
Research Interests:
Research Interests:
Research Interests: Thermodynamics, Stability, Macromolecular X-Ray Crystallography, Crystal structure, Animals, and 12 moreProtein structure, Enzyme, Hydrogen Bond, European, Amino Acid Sequence, Hydrogen-Ion Concentration, Protein Denaturation, Charge Distribution, Ions, Glutamic Acid, Biochemistry and cell biology, and Dimerization
Research Interests:
Research Interests:
Schistosoma japonicum glutathione S-transferase (SjGST) is a common fusion tag in recombinant protein production, and its 3-dimensional structure has been studied in the context of drug design. We have determined the crystal structure of... more
Schistosoma japonicum glutathione S-transferase (SjGST) is a common fusion tag in recombinant protein production, and its 3-dimensional structure has been studied in the context of drug design. We have determined the crystal structure of non-fused SjGST complexed with glutathione, and compare it to complexes between glutathione and SjGST fusion proteins.
Research Interests:
Research Interests:
Research Interests:
Research Interests:
Research Interests: Thermodynamics, Molecular Biology, Kinetics, Anisotropy, Molecular, and 21 moreCrystal structure, Mice, Animals, Alternative splicing, Proline, Structure Analysis, Hydrogen Bond, Hydrogen Bonding, High Resolution, Protein Secondary Structure Prediction, X ray diffraction, Alternative Splicing, Calorimetry, Molecular weight, Glutathione Transferase, Protein Binding, Ligands, Biochemistry and cell biology, Molecular Structure, Dimerization, and Cell Adhesion Molecules
Research Interests: Molecular Biology, Small Angle X Ray Scattering, Apoptosis, Macromolecular X-Ray Crystallography, Molecular, and 13 moreCrystal structure, Mice, Animals, Phosphorylation, Active site, Calmodulin, Protein Conformation, Protein Kinase, Drug Targeting, Solution Structure, Nucleotides, Biochemistry and cell biology, and Dimerization
Research Interests: Biological Chemistry, Multidisciplinary, Macromolecular X-Ray Crystallography, Anisotropy, Biological Sciences, and 21 moreCrystal structure, Animals, Drug Design, Proline, Enzyme, CHEMICAL SCIENCES, Hydrogen Bonding, Active site, Trypanosoma Cruzi, Amino Acid Profile, Protein Conformation, Amino Acid Sequence, Triosephosphate Isomerase, Protein Binding, Protons, Binding Site, Glutamic Acid, Histidine, Enzyme Catalysis, Solvents, and Dimerization
Apicomplexan parasites, such as the malaria-causing Plasmodium species, utilize a unique way of locomotion and host cell invasion. This substrate-dependent gliding motility requires rapid cycling of actin between the monomeric state and... more
Apicomplexan parasites, such as the malaria-causing Plasmodium species, utilize a unique way of locomotion and host cell invasion. This substrate-dependent gliding motility requires rapid cycling of actin between the monomeric state and very short, unbranched filaments. Despite the crucial role of actin polymerization for the survival of the malaria parasite, the majority of Plasmodium cellular actin is present in the monomeric form. Plasmodium lacks most of the canonical actin nucleators, and formins are essentially the only candidates for this function in all Apicomplexa. The malaria parasite has two formins, containing conserved formin homology (FH) 2 and rudimentary FH1 domains. Here, we show that Plasmodium falciparum formin 1 associates with and nucleates both mammalian and Plasmodium actin filaments. Although Plasmodium profilin alone sequesters actin monomers, thus inhibiting polymerization, its monomer-sequestering activity does not compete with the nucleating activity of f...
Research Interests:
Research Interests:
Research Interests:
Research Interests:
Research Interests:
Gene fusion is a common mechanism of protein evolution that has mainly been discussed in the context of multidomain or symmetric proteins. Less is known about fusion of ancestral genes to produce small single-domain proteins. Here, we... more
Gene fusion is a common mechanism of protein evolution that has mainly been discussed in the context of multidomain or symmetric proteins. Less is known about fusion of ancestral genes to produce small single-domain proteins. Here, we show with a domain-swapped mutant Plasmodium profilin that this small, globular, apparently single-domain protein consists of two foldons. The separation of binding sites for different protein ligands in the two halves suggests evolution via an ancient gene fusion event, analogous to the formation of multidomain proteins. Finally, the two fragments can be assembled together after expression as two separate gene products. The possibility to engineer both domain-swapped dimers and half-profilins that can be assembled back to a full profilin provides perspectives for engineering of novel protein folds, e.g., with different scaffolding functions.