Literature summary extracted from
Huet, S.; Avilov, S.V.; Ferbitz, L.; Daigle, N.; Cusack, S.; Ellenberg, J.
Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy (2010), J. Virol., 84, 1254-1264.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
2.7.7.48 |
RanBP5 |
a member of importin beta family, required for PB1/PA heterodimer import into the nucleus, where the active heterotrimer of the enzyme is formed |
influenza A virus |
|
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.7.48 |
additional information |
impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm |
influenza A virus |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
2.7.7.48 |
nucleus |
efficient polymerase assembly is a limiting factor in the viability of reassortant viruses, mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview. PB1 and PA form a dimer in the cytoplasm, which is imported into the nucleus, separately from PB2. The PB1/PA heterodimer is imported into the nucleus by RanBP5, a member of importin beta family. Once in the nucleus, the PB1/PA dimer associates with PB2 to form the trimeric polymerase |
influenza A virus |
5634 |
- |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.7.48 |
influenza A virus |
- |
- |
- |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.7.48 |
trimer |
mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview. PB1 and PA form a dimer in the cytoplasm, which is imported into the nucleus separately from PB2. Once in the nucleus, the PB1/PA dimer associates with PB2 to form the trimeric polymerase. The strong interface that can be formed between the N-terminal extremity of PB2 and the C-terminal extremity of PB1 is present only in the fully assembled trimeric polymerase |
influenza A virus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.7.48 |
RNA-dependent RNA polymerase |
- |
influenza A virus |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.7.7.48 |
malfunction |
impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm |
influenza A virus |
2.7.7.48 |
additional information |
efficient polymerase assembly is a limiting factor in the viability of reassortant viruses, mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview |
influenza A virus |