De Novo Synthesis of Plasma Membrane and Tonoplast Polypeptides of Barley Roots during Short-Term K+ Deprivation
Author(s) -
Mala Fernando,
Jarnail S. Mehroke,
Anthony D. M. Glass
Publication year - 1992
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.100.3.1269
Subject(s) - vacuole , membrane , term (time) , chemistry , biology , biochemistry , botany , microbiology and biotechnology , biophysics , physics , cytoplasm , quantum mechanics
[(35)S]Methionine labeling of intact barley roots (Hordeum vulgare cv Klondike) after short (6-12 h) and longer (18-24 and 90-96 h) periods of K(+) deprivation revealed that several membrane polypeptides were synthesized in significantly increased amounts following withdrawal of K(+) from nutrient solutions. One of these, a 43-kD polypeptide localized in plasma membrane- and tonoplast-enriched fractions, accounted for a large part of (35)S incorporation into membranes when [(35)S]methionine was administered for 6 h following 6 h of K(+) deprivation. With increasing duration of K(+) deprivation, (35)S incorporation into this 43-kD polypeptide decreased. This polypeptide, referred to as KR43, was not synthesized when NO(3) (-) or inorganic phosphate was removed or when Rb(+) was substituted for K(+). However, it was synthesized when K(+) was removed and replaced by an equivalent concentration of Na(+). The intrinsic nature of this polypeptide and the time course of changes in its expression, which correspond with changes of K(+)((86)Rb) influx associated with K(+) deprivation, provide evidence that this polypeptide may form part of the high-affinity K(+) transport system in barley roots. A possible role for this polypeptide is discussed in the context of changes in the subcellular distribution of K(+) in barley roots following interruption of K(+) supply. A 45-kD microsomal polypeptide, identified in earlier studies as a response to K(+) deprivation, is suggested to be an extrinsic protein, readily displaced from membranes by exposure to ethylenediaminetetraacetate.
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