Journal article

CHLOROPLAST PHOSPHOPROTEINS - PHOSPHORYLATION OF A 12-KDA STROMAL PROTEIN BY THE REDOX-CONTROLLED KINASE OF THYLAKOID MEMBRANES

P BHALLA, J BENNETT

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS | Published : 1987

Abstract

Activation of the redox-controlled protein kinase of thylakoid membranes is detectable in vivo by measuring radioisotope incorporation into the light-harvesting Chl a/b protein and four photosystem II proteins (8.3, 32, 34, and 44 kDa). In normal barley leaves, the kinase is active under both aerobic and anaerobic (N2) conditions, but in the Chl b-less chlorina f2 mutant it is active only under anaerobic conditions. The responsiveness of this enzyme in the mutant to changes in the gas phase has been exploited to distinguish its protein substrates from those of other leaf protein kinases. Most of the soluble phosphoproteins of normal and mutant leaves (including a conspicuously labeled 67-kDa..

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University of Melbourne Researchers