1999 Fiscal Year Final Research Report Summary
STRUCTURE-FUNCTION RELATIONSHIP OF VIRAL RNA DEPENDENT RNA POLYMERASE.
| Project/Area Number |
10670291
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Virology
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| Research Institution | Kurume University |
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Principal Investigator |
TOYODA Tetsuya KURUME UNIVERSITY, SCHOOL OF MEDICINE, VIROLOGY, PROFESSOR, 医学部, 教授 (00197972)
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| Project Period (FY) |
1998 – 1999
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| Keywords | INFLUENZA VIRUS / HEPATITIS C VIRUS / RNA POLYMERASE / SUBUNIT / PROTEASE |
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| Research Abstract |
The RNA-dependent NA polymerase of influenza A virus consists of three subunits, pB1, PB2 and PA. PB1 is a catalytic subunit of NA synthesis. PB2 confers a transcriptase activity to PB1. PA provides replicase activity and performs a recently identified unique protease activity. In order to map its functional domains, we generated site-specific antibodies. RNA synthesis activity was mapped in amino acids 1-159 of PB2 and 501-617 of PA. Cap-I dependent RNase activity was mapped in amino acids 1-159 and 305-559 of PB2, 1-222 of PB1, and 601-716 of PA. Cap-binding site was mapped in amino acids 402-559 of PB2.
We previously determined that the C-terminal 158 amino acids of PB1 bound to the N-termina1 249 amino acid stretch of PB2, while the N-terminal 140 amino acids ofPB1 bound to the C-terminal two third region of PA. This time, we have narrowed the PB1-PB2 binding site in 28 residues of PB2 and 180 residues of PB1, and the PB1-PA binding site in 25 residues of PB1 and about 200 residues of PA.
In order to expand our knowledge into other viral RNA-dependent RNA polymerases, we established in vitro transcription system of hepatitis C RNA polymerase.
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