2011 Fiscal Year Final Research Report
Structural basis for an essential subunit interaction in influenza virus RNA polymerase PB1-PB2
| Project/Area Number |
21370046
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Yokohama City University |
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Principal Investigator |
PARK Sam-yong 横浜市立大学, 生命ナノシステム科学研究科, 教授 (20291932)
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| Co-Investigator(Kenkyū-buntansha) |
FUKUNISHI Yoshihumi 産業技術総合研究所, バイオメディシナル情報研究センター, 主任研究員 (60357895)
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| Project Period (FY) |
2009 – 2011
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| Keywords | インフルエンザ / RNAポリメラーゼ / 構造解析 / 創薬 |
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| Research Abstract |
Influenza virus RNA-dependent RNA polymerase is a multi-functional heterotrimer, which uses a "cap-snatching" mechanism to produce viral mRNA. Host cell mRNA is cleaved to yield a cap-bearing oligonucleotide which can be extended using viral genomic RNA as a template. The cap binding and endonuclease activities are only activated once viral genomic RNA is bound. This requires signaling from the RNA-binding PB1 subunit to the cap-binding PB2 subunit, and the interface between these two subunits is essential for polymerase activity. We have defined this interaction surface by protein crystallography, and tested the effects of mutating contact residues on the function of the holo-enzyme. This novel interface is surprisingly small, yet it plays a crucial role in regulating the 250 kDa polymerase, and is completely conserved among avian and human influenza.
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Author(s)
Tachiwana H, Kagawa W, Shiga T, Osakabe A, Miya Y, Saito K, Hayashi-Takanaka Y, Oda T, Sato M, Park SY, Kimura H, Kurumizaka H.
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Journal Title
Nature
Volume: 476(7359)
Pages: 232-5
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Woo JS, Lim JH, Shin HC, Suh MK, Ku B, Lee KH, Joo K, Robinson H, Lee J, Park SY, Ha NC, Oh BH.
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Cell
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Pages: 85-96
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Author(s)
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Journal Title
Proc Natl Acad Sci U S A
Volume: 106(8)
Pages: 2612-6
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