Claim · model-written summary
AtPMT1 and AtPMT2 catalyse the symport of their substrates with protons in Xenopus oocytes.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianat0 - Gene
- AtPMT1 and AtPMT2e1
- Outcome
- symport of their substrates with protonse2
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e1“Expression of the AtPMT1 and AtPMT2 cDNAs in baker's yeast (Saccharomyces cerevisiae) revealed that these proteins catalyse the energy-dependent, high-capacity transport of fructose and xylitol, and the transport of several other compounds with lower rates”
e2“Expression of their cRNAs in Xenopus laevis oocytes showed that both proteins are voltage-dependent and catalyse the symport of their substrates with protons”
Title
Y.-S. Klepek; M. Volke; K. R. Konrad; et al. Journal of Experimental Botany 2009. doi:10.1093/jxb/erp322
Other claims from this paper (7)
- Observation AtPMT1 and AtPMT2 catalyse high-capacity transport of fructose and xylitol.
- Observation AtPMT1 and AtPMT2 transport several other compounds at lower rates.
- Observation AtPMT1 or AtPMT2 fused with GFP localized to Arabidopsis plasma membranes.
- Observation AtPMT2 reporter expression occurred in mature pollen grains.
- Observation AtPMT1 reporter expression occurred in germinating pollen grains.
- Observation AtPMT1 and AtPMT2 reporter expression occurred in growing pollen tubes, hydathodes, and young xylem cells.
- Observation Expression of AtPMT1 and AtPMT2 was confirmed with an anti-AtPMT1/AtPMT2 antiserum.