In vitro and in vivo protein phosphorylation in Avena sativa L. coleoptiles

Veluthambi, K. ; Poovaiah, B. W. (1986) In vitro and in vivo protein phosphorylation in Avena sativa L. coleoptiles Plant Physiology, 81 . pp. 836-841. ISSN 0032-0889

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In vitro and in vivo protein phosphorylations in oat (Avena sativa L.) coleoptile segments were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis and by two-dimensional gel electrophoresis. In vitro phosphorylation of several polypeptides was distinctly promoted at I to 15 micromolar free Ca2+ concentrations. Ca2+-stimulated phosphorylation was markedly reduced by trifluoperazine, chlorpromazine, and naphthalene sulfonamide (W7). Two polypeptides were phosphorylated both under in vitro and in vivo conditions, but the patterns of phosphorylation of several other polypeptides were different under the two conditions indicating that the in vivo phosphorylation pattern of proteins is not truly reflected by in vitro phosphorylation studies. Trifluoperazine, W7, or ethylene glycol-bis-(β,-aminoethyl ether)-N,N'-tetraacetic acid (EGTA) + calcium ionophore A23187 treatments resulted in reduced levels of in vivo protein phosphorylation of both control and auxin-treated coleoptile segments. Analysis by two-dimensional electrophoresis following in vivo phosphorylation revealed auxin-dependent changes of certain polypeptides. A general inhibition of phosphorylation by calmodulin antagonists suggested that both control and auxin-treated coleoptiles exhibited Ca2+, and calmodulin-dependent protein phosphorylation in vivo.

Item Type:Article
Source:Copyright of this article belongs to American Society of Plant Biologists.
ID Code:57249
Deposited On:26 Aug 2011 03:39
Last Modified:26 Aug 2011 03:39

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