Vol 88, No 12 (2023)
Articles
Editorial
Abstract
Changes in the glutamate/gaba system in the hippocampus of rats with age and during the Alzheimer’s disease signs development
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A new mouse strain with mutation in the NFE2L2 (NRF2 gene
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Role of mitochondrial DNA in yeast replicative aging
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Serotonin receptors - a potential target for the treatment of Alzheimer’s disease
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Role of ubiquitin-proteasome system in stem cell biology
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The role of Aurora B kinase in normal and cancer cells
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Topology of ubiquitin chains in the e3 ubiquitin ligase rnf168 chromatosome entourage
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Impact of lipid matrix composition on the activity of membranotropic enzymes galactonolactone oxidase from Trypanosoma cruzi and L-galactono-1,4-lactone dehydrogenase from Arabidopsis thaliana in the system of reverse micelles
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Low-frequency vibrations of bacteriochlorophyll oligomers in chlorosomes of photosynthetic green bacteria
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Effect of dexamethasone on human neutrophil adhesion and concomitant secretion
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Opposing effects of CRABP1 and CRABP2 homologs on the proliferation of breast cancer cells and their sensitivity to retinoic acid
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Dicarbonyl-modified low-density lipoproteins are key inducers of LOX-1 and NOX1 gene expression in cultured human umbilical vein endotheliocytes
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Nocistatin and products of its proteolysis as dual modulators of type 3 acid-sensing ion channels (ASIC3) with an algesic and analgesic effect
Abstract
Changes in the structure of potato virus A virions during limited proteolysis in situ according to tritium labeling data and computer simulation
Abstract
The coat proteins (CP) of potato virus A virions (PVA) contain partially disordered N-terminal domains, which are necessary for performing vital functions of the virus. A comparative analysis of the structures of coat proteins (CPs) in intact PVA virions and in virus particles lacking the N-terminal 32 amino acids (PVAΔ32) was carried out in this work based on the tritium planigraphy data. Using the atomic resolution structure of the potato virus Y potyvirus (PVY) protein, which is a homolog of CP PVA, the available CP surfaces in the PVY virion were calculated and the areas of intersubunit/ interhelix contacts were determined. For this purpose, the approach of Lee and Richards (Lee, B., and Richards, F. M. (1971) J. Mol. Biol., 55, 379-400) was used. Comparison of the incorporation profiles of the tritium label in intact and trypsin-degraded PVA∆32 revealed the position of the ΔN-peptide shielding the surface domain (a.a. 66-73, 141-146) and the interhelix zone (a.a. 161-175) of the PVA CP. The presence of channels/cavities was found in the virion, which turned out to be partially permeable to tritium atoms. Upon removal of the ∆N-peptide, a decrease in the label within the virion (a.a. 184-200) was also observed, indicating a possible structural transition leading to virion compactization. Based on the data obtained, we can conclude that part of the surface ∆N-peptide is located between the coils of the virion helix, which increases the helix pitch and provides greater flexibility of the virion, which is important for the intercellular transport of the viruses in the plants.