EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
|---|
   3.4.22.29 | -999 |
- |
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 |
701390 |
| 3.4.22.29 | -999 |
- |
around 50% cleavage of cellular eukaryotic translation initiation factor eIF4GI is obtained at 4 h postinfection |
699915 |
| 3.4.22.29 | -999 |
- |
at 6 h and 8 h postinfection, cellular eukaryotic translation initiation factor eIF4GI is nearly completely processed into its typical cleavage products |
699915 |
| 3.4.22.29 | -999 |
- |
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 |
701390 |
| 3.4.22.29 | -999 |
- |
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 |
699905 |
| 3.4.22.29 | -999 |
- |
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 |
699905 |
| 3.4.22.29 | -999 |
- |
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 |
701198 |
| 3.4.22.29 | -999 |
- |
low concentrations of 2Apro produce complete cleavage of eIF4GI in less than 5 min, producing several cleavage products from the multiple eIF4GI isoforms |
699905 |
| 3.4.22.29 | -999 |
- |
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 |
701198 |
| 3.4.22.29 | -999 |
- |
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 |
701390 |
