More data about this group.
Last database update for these data: 2008-06-04 - Data extracted on 2009-04-14 from the database.
| Field | Value |
|---|---|
| Document type | Journal article: paper |
| Language | English |
| Year | 2003 |
| Authors | Plisson, C. Drucker, M. Blanc, S. German-Retana, S. Le Gall, O. Thomas, D. Bron, P. |
| Title | Structural characterization of HC-Pro, a plant virus multifunctional protein |
| Source | J. Biol. Chem. |
| Volume | 278 |
| Issue | 26 |
| Pages | 23753-23761 |
| Abstract | The helper component proteinase (HC-Pro) is a key protein encoded by plant viruses of the genus Potyvirus. HC-Pro is involved in different steps of the viral cycle, aphid transmission, replication, and virus cell-to-cell and systemic movement and is a suppressor of post-transcriptional gene silencing. Structural knowledge of HC-Pro is required to better understand its multiple functions. To this aim, we purified His-tagged wild-type HC-Pro and a N-terminal deletion mutant (DeltaHC-Pro) from plants infected with recombinant potyviruses. Biochemical analysis of the recombinant proteins confirmed that HC-Pro is a dimer in solution, that the N terminus is not essential for self-interaction, and that a large C-terminal domain is highly resistant to proteolysis. Two-dimensional crystals of the recombinant proteins were successfully grown on Ni2+-chelating lipid monolayers. Comparison of projection maps of negatively stained crystals revealed that HC-Pro is composed of two domains separated by a flexible constriction. Cryo-electron crystallography of DeltaHC-Pro allowed us to calculate a projection map at 9-A resolution. Our data from electron microscopy, biochemical analysis, and secondary structure predictions lead us to suggest a model for structure/function relationships in the HC-Pro protein. |
| Web page | Web page Pubmed |
| ISSN | 0021-9258 |