Kuvaus
| Alkuperäiskieli | englanti |
|---|---|
| Sivut | 46 |
| Sivumäärä | 1 |
| Tila | Julkaistu - 2017 |
| Tapahtuma | Instruct Biennial Structural Biology Conference 2017 - International Best Western Hotel, Brno, Tšekki Kesto: 24 toukokuuta 2017 → 26 toukokuuta 2017 https://www.structuralbiology.eu/biennial2017 |
Konferenssi
| Konferenssi | Instruct Biennial Structural Biology Conference 2017 |
|---|---|
| Lyhennettä | IBSBM2017 |
| Maa | Tšekki |
| Kaupunki | Brno |
| Ajanjakso | 24/05/2017 → 26/05/2017 |
| www-osoite |
Tieteenalat
- 1182 Biokemia, solu- ja molekyylibiologia
Lainaa tätä
, Brno, Tšekki.
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, Brno, Tšekki, 24/05/2017 - 26/05/2017, Sivut 46.
Structural insights into phosphoprotein chaperoning of nucleoprotein in measles virus. / Guryanov, Sergey; Liljeroos, Lassi Juho Petteri; Kasaragod, Prasad; Kajander, Tommi Antero; Butcher, Sarah Jane.
2017. 46 Posterin esittämispaikka: Instruct Biennial Structural Biology Conference 2017, Brno, Tšekki.
Tutkimustuotos: Konferenssimateriaalit › Posteri › Tutkimus
TY - CONF
T1 - Structural insights into phosphoprotein chaperoning of nucleoprotein in measles virus
AU - Guryanov, Sergey
AU - Liljeroos, Lassi Juho Petteri
AU - Kasaragod, Prasad
AU - Kajander, Tommi Antero
AU - Butcher, Sarah Jane
N1 - Instruct Biennial Structural Biology Conference Abstract Booklet
PY - 2017
Y1 - 2017
N2 - Measles virus is an important, highly contagious, human pathogen. The nucleoprotein N binds only to viral genomic RNA and forms the helical ribonucleocapsid that serves as a template for viral replication. We address how N is regulated by another protein, the phosphoprotein, P, to prevent newly synthesized N from binding to cellular RNA. Here, we pulled down an N01-408 fragment lacking most of its C-terminal tail domain by several affinity-tagged, N-terminal, P fragments to map the N0-binding region of P to the first 48 amino acids. We showed biochemically and using P mutants the importance of the hydrophobic interactions for the binding. We fused an N0 binding peptide, P1-48, to the C-terminus of an N021-408 fragment lacking both the N-terminal peptide and the C-terminal tail of N protein to reconstitute and crystallize the N0-P complex. We solved the X-ray structure of the resulting N0-P chimeric protein at 2.7 Å resolution. The structure reveals the molecular details of the conserved N0-P interface and explains how P chaperones N0 preventing both self-assembly of N0 and its binding to RNA. We compare the structure of an N0-P complex to atomic model of helical ribonucleocapsid. We thus propose a model how P may help to start viral RNA synthesis. Our results provide a new insight into mechanisms of paramyxovirus replication. New data on the mechanisms of phosphoprotein chaperone action allows better understanding of the virus genome replication and nucleocapsid assembly. We describe a conserved structural interface for the N-P interaction which could be a target for drug development not only to treat measles but also potentially other paramyxovirus diseases.
AB - Measles virus is an important, highly contagious, human pathogen. The nucleoprotein N binds only to viral genomic RNA and forms the helical ribonucleocapsid that serves as a template for viral replication. We address how N is regulated by another protein, the phosphoprotein, P, to prevent newly synthesized N from binding to cellular RNA. Here, we pulled down an N01-408 fragment lacking most of its C-terminal tail domain by several affinity-tagged, N-terminal, P fragments to map the N0-binding region of P to the first 48 amino acids. We showed biochemically and using P mutants the importance of the hydrophobic interactions for the binding. We fused an N0 binding peptide, P1-48, to the C-terminus of an N021-408 fragment lacking both the N-terminal peptide and the C-terminal tail of N protein to reconstitute and crystallize the N0-P complex. We solved the X-ray structure of the resulting N0-P chimeric protein at 2.7 Å resolution. The structure reveals the molecular details of the conserved N0-P interface and explains how P chaperones N0 preventing both self-assembly of N0 and its binding to RNA. We compare the structure of an N0-P complex to atomic model of helical ribonucleocapsid. We thus propose a model how P may help to start viral RNA synthesis. Our results provide a new insight into mechanisms of paramyxovirus replication. New data on the mechanisms of phosphoprotein chaperone action allows better understanding of the virus genome replication and nucleocapsid assembly. We describe a conserved structural interface for the N-P interaction which could be a target for drug development not only to treat measles but also potentially other paramyxovirus diseases.
KW - 1182 Biochemistry, cell and molecular biology
M3 - Poster
SP - 46
ER -
, Brno, Tšekki.