3.4.22.29: picornain 2A
This is an abbreviated version!
For detailed information about picornain 2A, go to the full flat file.
Reaction
selective cleavage of Tyr-/-Gly bond in picornavirus polyprotein
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Synonyms
2A cysteine protease, 2A protease, 2A proteinase, 2Apro, coxsackievirus B3 2A protease, CV-B3 proteinase 2A, CVB3 2A, enterovirus 2A protease, EV-A71 2Apro, EV71-2A, HRV 2A protease, HRV16 2A, HRVC15 2Apro, P2A, picornaviral 2A protein, picornaviral 2A proteinase, picornavirus 2A proteinase, picornavirus endopeptidase 2A, poliovirus 2A protease, poliovirus 2Apro, poliovirus protease 2A, poliovirus protease 2Apro, protease 2A, proteinase 2A, proteinase 2Apro, proteinase, poliovirus, 2A, PV 2Apro, rhinovirus protease 2A, ubiquitin-specific protease 2a, USP2a, Y-G proteinase 2A
ECTree
Specific Activity
Specific Activity on EC 3.4.22.29 - picornain 2A
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8.8
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human rhinovirus type 2
additional information
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addition of increasing concentrations of PABP-interacting protein 1 do not affect 2Apro-mediated cleavage of poly(A) binding protein, at the highest concentration (3 microg) of PABP-interacting protein 1 tested, increasing concentrations of 2Apro (0.5-1.5 microg) lead to a dose-dependent increase in cleavage of poly(A) binding protein by 2Apro proteinase
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cleavage kinetics analysis indicates that poly(A) binding protein exists in multiple conformations, some of which are resistant to 2Apro cleavage and can be modulated by reducing potential
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cleavage of poly(A)-binding protein by 2Apro is incomplete, a single 2Apro cleavage product can be observed late in the reaction, and 8fold-higher levels of 2A protease produce only marginally higher levels of cleavage
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combined 2Apro and 3Cpro result in a net stimulation of poliovirus internal ribosome entry site-mediated translation, the resulting rate of translation is about 3fold greater than the control value but not as great as the 4fold stimulation of translation from preincubation with 2Apro alone
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low concentrations of 2Apro produce complete cleavage of eIF4GI in less than 5 min, producing several cleavage products from the multiple eIF4GI isoforms
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poly(A) binding protein in a HeLa S10 lysate is also highly resistant to cleavage by 2Apro despite high 2Apro activity versus eIF4GI, the initial cleavage rate is very slow and remains constant for 60 min before slowing down further upon extended incubation. Extended incubation also reveals a biphasic cleavage profile, incubation of 2Apro with recombinant His-poly(A) binding protein results in relatively poor and variable cleavage ranging from 0-20%, this suggested that most purified protein usually exists in a conformation not suitable for 2Apro recognition and binding
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around 50% cleavage of cellular eukaryotic translation initiation factor eIF4GI is obtained at 4 h postinfection
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at 6 h and 8 h postinfection, cellular eukaryotic translation initiation factor eIF4GI is nearly completely processed into its typical cleavage products
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in the presence of the 2A protease, the Rluc expression from the mutant encephalomyocarditis virus internal ribosome entry site elements is strongly reduced suggesting that the residual translation (seen in the absence of 2A) is occurring principally by a cap-dependent mechanism
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monocistronic RNAs containing the avian encephalomyelitis virus IRES elements with mutations in the stem 1 or stem 2 of the pseudoknot are also very efficiently translated when assayed alone, but this expression is essentially eliminated in the presence of 2A protease
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when a dicistronic vector containing the Fluc coding sequence upstream of the wild type encephalomyocarditis virus internal ribosome entry site elements is assayed, it is shown that the encephalomyocarditis virus IRES-directed Rluc expression is unaffected by the coexpression of the 2A protease, but the expression of the upstream open reading frame is strongly inhibited