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Literature summary for 3.4.22.29 extracted from

  • Yang, X.; Hu, Z.; Fan, S.; Zhang, Q.; Zhong, Y.; Guo, D.; Qin, Y.; Chen, M.
    Picornavirus 2A protease regulates stress granule formation to facilitate viral translation (2018), PLoS Pathog., 14, e1006901 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.29

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type enzyme and mutant 2AC110S in HeLa cells Enterovirus A71

Protein Variants

Protein Variants Comment Organism
C110S construction of catalytically inactive enzyme mutant EV71-2AC110S Enterovirus A71

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
eukaryotic translation initiation factor 4G + H2O Enterovirus A71 eIF4G ?
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 ?
eukaryotic translation initiation factor 4G + H2O Enterovirus A71 BrCR eIF4G ?
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 ?

Organism

Organism UniProt Comment Textmining
Enterovirus A71 Q66478 EV71
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Enterovirus A71 BrCR Q66478 EV71
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Source Tissue

Source Tissue Comment Organism Textmining
additional information the virus is propagated in HeLa cells Enterovirus A71
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
eukaryotic translation initiation factor 4G + H2O eIF4G Enterovirus A71 ?
-
 ?
eukaryotic translation initiation factor 4G + H2O eIF4G Enterovirus A71 BrCR ?
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 ?
additional information no activity with mutant substrates PABPM490P/Q540N and eIF4GIG689E Enterovirus A71 ?
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 ?
additional information no activity with mutant substrates PABPM490P/Q540N and eIF4GIG689E Enterovirus A71 BrCR ?
-
 ?
polyadenylate-binding protein 1 + H2O PABP Enterovirus A71 ?
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 ?
polyadenylate-binding protein 1 + H2O PABP Enterovirus A71 BrCR ?
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 ?

Synonyms

Synonyms Comment Organism
2A protease
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 Enterovirus A71
EV71-2A
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 Enterovirus A71

General Information

General Information Comment Organism
malfunction infection of 2A protease activity-inactivated recombinant EV71 (EV71-2AC110S) failed to induce atypical stress granule (aSG) formation and only induced typical stress granule (tSG) formation, which is PKR and eIF2alpha phosphorylation-dependent. When the protease activity of 2A in EV71 is blocked (EV71-2AC110S), the tSGs but not aSGs appear in infected cells Enterovirus A71
additional information the 2A proteases of other picornaviruses such as poliovirus and coxsackievirus also induce aSG formation and blocked tSG formation Enterovirus A71
physiological function the 2A protease of enterovrius 71 (EV71) induces atypical stress granule (aSG), but not typical stress granule (tSG) formation, via cleavage of eIF4GI. Furthermore, 2A is required and sufficient to inhibit tSGs formation induced by EV71 infection, sodium arsenite, or heat shock. EV71-induced aSGs are beneficial to viral translation through sequestering only cellular mRNAs, but not viral mRNAs. Thus, EV71 infection induces tSG formation via the PKR-eIF2alpha pathway, and on the other hand, 2A, but not 3C protease (EC 3.4.22.28), blocks tSG formation Enterovirus A71