Claim · model-written summary
In the presence of RCNMV RNA1, the NbGAPDH-A fusion protein localized to the cortical VRC as well as the chloroplasts.
- Outcome
- localized to the cortical VRC as well as the chloroplastse0
- Qualifier
- In the presence of RCNMV RNA1e0
Not reportedTaxonMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValue
Verbatim
e0“In the presence of RCNMV RNA1, however, the protein localized to the cortical VRC as well as the chloroplasts”
Title
Masanori Kaido; Kazutomo Abe; Akira Mine; et al. PLoS Pathogens 2014. doi:10.1371/journal.ppat.1004505
Other claims from this paper (8)
- Observation Cortical punctate structures containing the movement protein constitute a viral replication complex of RCNMV, in addition to aggregate structures adjacent to the nucleus.
- Observation NbGAPDH-A was identified as a host protein interacting with the RCNMV movement protein in infected Nicotiana benthamiana leaves.
- Intervention effect Virus-induced gene silencing of NbGAPDH-A reduced RCNMV multiplication in inoculated leaves.
- Intervention effect Silencing of NbGAPDH-A did not reduce RCNMV multiplication in single cells.
- Mechanism The authors suggest that GAPDH-A plays a positive role in cell-to-cell movement of RCNMV.
- Observation The NbGAPDH-A-GFP fusion protein localized exclusively to chloroplasts.
- Observation Bimolecular fluorescence complementation and GST pulldown assays confirmed in vivo and in vitro interactions, respectively, between the RCNMV movement protein and NbGAPDH-A.
- Intervention effect Gene silencing of NbGAPDH-A inhibited localization of the movement protein to the cortical VRC.