Protein phosphorylation in pea [Pisum sativum] root plastids

Protein phosphorylation has been investigated in nonphotosynthetic plastids of pea roots. Intact and lysed preparations of plastids were incubated with [gamma-32P]ATP and three stromal proteins of sizes 41, 58 and 62 kDa were phosphorylated on a serine residue. No other proteins were significantly l...

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Bibliographic Details
Published in:	Plant and cell physiology Vol. 42; no. 6; pp. 642 - 649
Main Authors:	Lukaszewski, K.M. (University of Manchester (UK)), Bowsher, C.G, Savory, P.J, Emes, M.J
Format:	Journal Article
Language:	English
Published:	Japan Oxford University Press 01-06-2001 Oxford Publishing Limited (England)
Subjects:	3 phosphoglyeric acid Adenosine Triphosphate - metabolism BIOCHEMICAL PATHWAYS DHAP dihydroxyacetone phosphate Glc1P Glc6P glucose 1-phosphate glucose 6-phosphate Glucose-6-Phosphate - metabolism Hydrogen-Ion Concentration Key words: Pisum sativum — Plastids — Protein phosphorylation — Roots Magnesium - metabolism methyl viologen Nitrites - metabolism OPPP oxidative pentose phosphate pathway PEP PGA PGM phosphoenolpyruvic acid phosphoglucomutase Phosphoproteins - metabolism PHOSPHORYLATION PISUM SATIVUM Pisum sativum - metabolism Plant Proteins - metabolism Plant Roots - metabolism PLASTIDS Plastids - metabolism PROTEINS ROOTS
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