Claim · model-written summary
The authors suggest the Hsp90-SGT1 complex regulates Tm-2(2) stability as a chaperone in TMV resistance.
- Taxon
- N.benthamianae1
- Interactor
- TMV
Tobacco mosaic viruse0pathogen - Gene
- Tm-2(2)e0
- Outcome
- Tm-2(2)-mediated TMV resistancee0
- Qualifier
- functioning as chaperone to regulate Tm-2(2) stabilitye0
Not reportedMaterialCompoundOrgan / stageSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValue
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Hsp90-SGT1 complex takes part in Tm-2(2)-mediated TMV resistance by functioning as chaperone to regulate Tm-2(2) stability”
e1“the N.benthamiana Heat shock protein 90 (Hsp90)”
Title
Hsp90 Interacts With Tm-22 and Is Essential for Tm-22-Mediated Resistance to Tobacco mosaic virus
Lichao Qian; Jinping Zhao; Yumei Du; et al. Frontiers in Plant Science 2018. doi:10.3389/fpls.2018.00411
Other claims from this paper (4)
- Observation N.benthamiana Hsp90 specifically interacts with Tm-2(2).
- Intervention effect Silencing Hsp90 compromised Tm-2(2)-mediated resistance to TMV.
- Intervention effect Silencing Hsp90 reduced steady-state Tm-2(2) protein levels.
- Observation Hsp90 associates with SGT1 in yeast and plant cells.