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Title: Potassium-dependent changes in the expression of membrane-associated proteins in barley roots

Journal Article · · Plant Physiology; (USA)
DOI:https://doi.org/10.1104/pp.92.4.1128· OSTI ID:5923338
; ; ;  [1]
  1. Univ. of British Columbia, Vancouver (Canada)

Barley (Hordeum vulgare L. cv Halcyon) seedlings which has been grown in full strength complete inorganic nutrient media (containing 6 millimolar K{sup +}) had high internal K{sup +} concentrations and low values of K{sup +} ({sup 86}Rb{sup +}) influx when influx was measured from solutions containing 100 micromolar K{sup +}. Transfer of these plants to solutions lacking K{sup +} resulted in significant reductions of root and shoot K{sup +} concentrations and values of K{sup +} ({sup 86}Rb{sup +}) influx increased by greater than 10-fold within 3 days. When plants treated in this way were returned to complete solutions, containing K{sup +}, the changes induced by K{sup +} deprivation were reversed. Parallel studies of microsomal membranes by means of SDS-PAGE demonstrated that the expression of a group of polypeptides increased or decreased in parallel with changes of K{sup +} ({sup 86}Rb{sup +}) influx. Most prominent of these were 45 and 34 kilodalton polypeptides which specifically responded to K{sup +} status of the barley plants; their expression was not enhanced by N or P deprivation. The 45 kilodalton polypeptide was susceptible to degradation by a membrane associated protease when microsomes were washing in buffer containing 0.2 millimolar PMSF. This loss was prevented by increasing PMSF concentration to 2 millimolar.

OSTI ID:
5923338
Journal Information:
Plant Physiology; (USA), Vol. 92:4; ISSN 0032-0889
Country of Publication:
United States
Language:
English