Influenza virus RNA polymerase PA subunit is a novel serine protease with Ser624 at the active site
Background Influenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the influenza virus RNA polymerase PA subunit in viral replication is poorly understood, although the enzyme is known to be required for cRNA → v...
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| Published in | Genes to cells : devoted to molecular & cellular mechanisms Vol. 6; no. 2; pp. 87 - 97 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
Blackwell Science Ltd
01.02.2001
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Background
Influenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the influenza virus RNA polymerase PA subunit in viral replication is poorly understood, although the enzyme is known to be required for cRNA → vRNA synthesis. The protease related activity of PA has been discussed ever since protease‐inducing activity was demonstrated in transfection experiments.
Results
PA protein was highly purified from insect cells infected with the recombinant baculovirus carrying PA cDNA, and a novel chymotrypsin‐type serine protease activity was identified with the synthetic peptide, Suc‐LLVY‐MCA, in the PA protein. [3H]DFP was crosslinked with PA and a mutational analysis revealed that serine624 was as an active site for the protease activity.
Conclusions
These results constitute the demonstration of protease activity in PA subunit of the influenza virus RNA polymerase complexes. |
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| AbstractList | Background
Influenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the influenza virus RNA polymerase PA subunit in viral replication is poorly understood, although the enzyme is known to be required for cRNA → vRNA synthesis. The protease related activity of PA has been discussed ever since protease‐inducing activity was demonstrated in transfection experiments.
Results
PA protein was highly purified from insect cells infected with the recombinant baculovirus carrying PA cDNA, and a novel chymotrypsin‐type serine protease activity was identified with the synthetic peptide, Suc‐LLVY‐MCA, in the PA protein. [
3
H]DFP was crosslinked with PA and a mutational analysis revealed that serine624 was as an active site for the protease activity.
Conclusions
These results constitute the demonstration of protease activity in PA subunit of the influenza virus RNA polymerase complexes. Influenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the influenza virus RNA polymerase PA subunit in viral replication is poorly understood, although the enzyme is known to be required for cRNA arrow right vRNA synthesis. The protease related activity of PA has been discussed ever since protease-inducing activity was demonstrated in transfection experiments. PA protein was highly purified from insect cells infected with the recombinant baculovirus carrying PA cDNA, and a novel chymotrypsin-type serine protease activity was identified with the synthetic peptide, Suc-LLVY-MCA, in the PA protein. [ super(3)H]DFP was crosslinked with PA and a mutational analysis revealed that serine624 was as an active site for the protease activity. These results constitute the demonstration of protease activity in PA subunit of the influenza virus RNA polymerase complexes. BACKGROUNDInfluenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the influenza virus RNA polymerase PA subunit in viral replication is poorly understood, although the enzyme is known to be required for cRNA --> vRNA synthesis. The protease related activity of PA has been discussed ever since protease-inducing activity was demonstrated in transfection experiments. RESULTSPA protein was highly purified from insect cells infected with the recombinant baculovirus carrying PA cDNA, and a novel chymotrypsin-type serine protease activity was identified with the synthetic peptide, Suc-LLVY-MCA, in the PA protein. [3H]DFP was crosslinked with PA and a mutational analysis revealed that serine624 was as an active site for the protease activity. CONCLUSIONSThese results constitute the demonstration of protease activity in PA subunit of the influenza virus RNA polymerase complexes. Background Influenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the influenza virus RNA polymerase PA subunit in viral replication is poorly understood, although the enzyme is known to be required for cRNA → vRNA synthesis. The protease related activity of PA has been discussed ever since protease‐inducing activity was demonstrated in transfection experiments. Results PA protein was highly purified from insect cells infected with the recombinant baculovirus carrying PA cDNA, and a novel chymotrypsin‐type serine protease activity was identified with the synthetic peptide, Suc‐LLVY‐MCA, in the PA protein. [3H]DFP was crosslinked with PA and a mutational analysis revealed that serine624 was as an active site for the protease activity. Conclusions These results constitute the demonstration of protease activity in PA subunit of the influenza virus RNA polymerase complexes. Influenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the influenza virus RNA polymerase PA subunit in viral replication is poorly understood, although the enzyme is known to be required for cRNA --> vRNA synthesis. The protease related activity of PA has been discussed ever since protease-inducing activity was demonstrated in transfection experiments. PA protein was highly purified from insect cells infected with the recombinant baculovirus carrying PA cDNA, and a novel chymotrypsin-type serine protease activity was identified with the synthetic peptide, Suc-LLVY-MCA, in the PA protein. [3H]DFP was crosslinked with PA and a mutational analysis revealed that serine624 was as an active site for the protease activity. These results constitute the demonstration of protease activity in PA subunit of the influenza virus RNA polymerase complexes. |
| Author | Iwahashi, Jun Mizoue, Kazutoshi Ohtsu, Yasushi Toyoda, Tetsuya Shiota, Mayumi Kido, Hiroshi Hamada, Nobuyuki Hara, Koyu Tsumura, Naoki Kashiwagi, Takahito Kato, Hirohisa |
| Author_xml | – sequence: 1 givenname: Koyu surname: Hara fullname: Hara, Koyu – sequence: 2 givenname: Mayumi surname: Shiota fullname: Shiota, Mayumi – sequence: 3 givenname: Hiroshi surname: Kido fullname: Kido, Hiroshi – sequence: 4 givenname: Yasushi surname: Ohtsu fullname: Ohtsu, Yasushi – sequence: 5 givenname: Takahito surname: Kashiwagi fullname: Kashiwagi, Takahito – sequence: 6 givenname: Jun surname: Iwahashi fullname: Iwahashi, Jun – sequence: 7 givenname: Nobuyuki surname: Hamada fullname: Hamada, Nobuyuki – sequence: 8 givenname: Kazutoshi surname: Mizoue fullname: Mizoue, Kazutoshi – sequence: 9 givenname: Naoki surname: Tsumura fullname: Tsumura, Naoki – sequence: 10 givenname: Hirohisa surname: Kato fullname: Kato, Hirohisa – sequence: 11 givenname: Tetsuya surname: Toyoda fullname: Toyoda, Tetsuya |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11260254$$D View this record in MEDLINE/PubMed |
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Influenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the... Influenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the influenza... BACKGROUNDInfluenza virus RNA polymerase is a multifunctional enzyme that catalyses both transcription and replication of the RNA genome. The function of the... |
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| SubjectTerms | Amino Acid Sequence Animals Base Sequence Binding Sites Catalysis Chromatography, Liquid DNA Primers DNA-Directed RNA Polymerases - chemistry DNA-Directed RNA Polymerases - genetics DNA-Directed RNA Polymerases - isolation & purification DNA-Directed RNA Polymerases - metabolism Electrophoresis, Polyacrylamide Gel Hydrogen-Ion Concentration Hydrolysis Influenza virus Orthomyxoviridae - enzymology Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Serine - metabolism Serine Endopeptidases - chemistry Serine Endopeptidases - genetics Serine Endopeptidases - isolation & purification Serine Endopeptidases - metabolism Spodoptera |
| Title | Influenza virus RNA polymerase PA subunit is a novel serine protease with Ser624 at the active site |
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