Osmoregulation in Lilium pollen grains occurs via modulation of the plasma membrane H+ ATPase activity by 14-3-3 proteins.
To allow successful germination and growth of a pollen tube, mature and dehydrated pollen grains (PGs) take up water and have to adjust their turgor pressure according to the water potential of the surrounding stigma surface. The turgor pressure of PGs of lily (Lilium longiflorum) was measured with a modified pressure probe for simultaneous recordings of turgor pressure and membrane potential to investigate the relation between water and electrogenic ion transport in osmoregulation. Upon hyperosmolar shock, the turgor pressure decreased, and the plasma membrane (PM) hyperpolarizes in parallel, whereas depolarization of the PM was observed with hypoosmolar treatment. An acidification and alkalinization of the external medium was monitored after hyper- and hypoosmotic treatments, respectively, and pH changes were blocked by vanadate, indicating a putative role of the PM H(+) ATPase. Indeed, an increase in PM-associated 14-3-3 proteins and an increase in PM H(+) ATPase activity were detected in PGs challenged by hyperosmolar medium. We therefore suggest that in PGs the PM H(+) ATPase via modulation of its activity by 14-3-3 proteins is involved in the regulation of turgor pressure.
Plant Molecular Biophysics and Biochemistry, Department of Molecular Biology, University of Salzburg, 5020 Salzburg, Austria.
Heidi
H
Pertl
Magdalena
M
Pöckl
Christian
C
Blaschke
Gerhard
G
Obermeyer
D048948:14-3-3 Proteins / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D027762:Lilium / Q000201:enzymology / Q000378:metabolism / Q000502:physiology*; D008564:Membrane Potentials; D009997:Osmotic Pressure; D011058:Pollen
D048948:14-3-3 Proteins; D000251:Adenosine Triphosphatases