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Plant and Cell Physiology, 2001, Vol. 42, No. 6 642-649
© 2001 Oxford University Press

Protein Phosphorylation in Pea Root Plastids

Katherine Marie Lukaszewski, Caroline Grace Bowsher, Peter John Savory and Michael James Emes1 School of Biological Sciences, 3.614 Stopford Building, University of Manchester, Oxford Road, Manchester, M13 9PL, U.K.

Protein phosphorylation has been investigated in non-photosynthetic 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 labelled under the conditions used. The 62 kDa protein is probably phosphoglucomutase and represents a phosphoenzyme catalytic intermediate. The protein kinase(s) and phosphatase(s) acting on the other proteins were not sensitive to exogenous calcium but were sensitive to magnesium. The protein phosphatase which acts on the 41 kDa protein is possibly of type 2C, whereas that acting on the 58 kDa phosphoprotein did not fall into any class defined by mammalian systems. Metabolism of exogenous glucose 6-phosphate by the oxidative pentose phosphate pathway in intact plastids abolished the phosphorylation of the 58 kDa protein. Dihydroxyacetone phosphate, phosphoenolpyruvate and 3-phosphoglycerate also inhibited phosphorylation of the 58 kDa protein and had a time-dependent effect on the phosphorylation of the 41 kDa protein. The significance of these results in relation to a possible role for protein phosphorylation in these plastids is considered.

1 Corresponding author: E-mail, mike.emes@man.ac.uk; Fax, +44-161-275-3938.


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