3.4.22.44: nuclear-inclusion-a endopeptidase
This is an abbreviated version!
For detailed information about nuclear-inclusion-a endopeptidase, go to the full flat file.
Reaction
Hydrolyses glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-/-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
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Synonyms
49 kDa proteinase, 49 kDa-Pro, NIA, NIa protease, NIa protein, NIa proteins, NIa-Pro, nuclear inclusion a protease, nuclear inclusion a-protease, nuclear inclusion body protein a, nuclear inclusion protein A protease, nuclear inclusion protein-a protease, nuclear inclusion-a protease, potyviral nuclear inclusion a, potyvirus NIa protease, protease NIa, proteinase Nia, proteinase, polyprotein-processing, Nia, proteins (specific proteins and subclasses), NIa (nuclear inclusion, a), proteins NIa, proteins, small nuclear inclusion NIa, tobacco vein mottling virus protease
ECTree
General Information
General Information on EC 3.4.22.44 - nuclear-inclusion-a endopeptidase
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physiological function
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the nuclear inclusion a protease of turnip mosaic virus is responsible for the processing of the viral polyprotein into functional proteins. Degradation of Amyloid-beta in the cytoplasm can be a novel strategy to control the levels of Amyloid-beta, plaque formation, and the associated cell death
physiological function
the TVMV genome is translated into a single large polyprotein that is subsequently processed by three virally encoded proteases. Seven of the nine cleavage events are carried out by the NIa protease
physiological function
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oligomeric amyloid beta-induced cytotoxicity and mitochondrial dysfunction are significantly ameliorated by the enzyme. The enzyme prevents mitochondrial deposition of amyloid beta
physiological function
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potyviral protein genome-linked, established as an intrinsically disordered domain, undergoes plausible structural alterations upon interaction with globular nuclear inclusion-a protease which induces the ATPase activity
physiological function
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protease NIa not only reduces amyloid-beta pathology, but also improves behavioral deficits in mice
physiological function
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the nuclear inclusion a-protease domain increases Myzus persicae growth and reproduction on both Nicotiana benthamiana and Arabidopsis thaliana
physiological function
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NIa-Pro responds to the presence of the aphid vector during infection by relocalizing to the vacuole. Remarkably, vacuolar localization is required for the ability of NIa-Pro to enhance aphid reproduction on host plants, vacuole localization disappears when aphids are removed
physiological function
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potyviral NIa targets many host elements during infection, establishing a network in which information is efficiently transmitted
additional information
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overexpression of NIa in rat B103 neuroblastoma cells results in a significant reduction in cell death caused by both intracellularly generated and exogenously added Amyloidbeta. Moreover, lentiviral-mediated expression of NIa in APPsw/PS1 transgenic mice significantly reduces the levels of Amyloid-beta and plaques in the brain
additional information
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the full-length potyviral genome protease, VPg-Pro, has two domains: an N-terminal viral protein genome-linked, VPg, and a C-terminal protease NIa-Pro. Regulation of nuclear inclusion protein-a protease is crucial for polyprotein processing and hence, for successful infection by potyviruses, mechanisms regulating nuclear inclusion protein-a protease activity. Firstly, the influence of the VPg domain on the proteolytic activity of NIa-Pro increases when the two domains interact each other. Secondly, the protease activity of NIa-Pro can also be modulated by phosphorylation at Ser129. interaction with VPg as well as phosphorylation of Ser129 relays a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro, molecular modeling, homology modeling, and molecular dynamics simulations, overview