Nucleic Acids Research, Vol 25, Issue 12 2403-2408, Copyright © 1997 by Oxford University Press
K Liere and G Link
Chloroplast RNA-binding protein p54 is an endoribonuclease required for
3'end-processing of plastid precursor transcripts. We find that purified
p54 can serve as a phosphate acceptor for protein kinases in vitro. Both
the processing and RNA-binding activities of p54 are enhanced by
phosphorylation and decreased by dephosphorylation. In addition, the enzyme
is activated by the oxidized form of glutathione and inhibited by the
reduced form, whereas other redox reagents that were tested showed no
effect. Kinase treatment of p54 prior to oxidation by glutathione resulted
in highest levels of activation, suggesting that phosphorylation and redox
state act together to control p54 activity in vitro and possibly also in
vivo.
ARTICLES
Chloroplast endoribonuclease p54 involved in RNA 3'-end processing is regulated by phosphorylation and redox state
Plant Cell Physiology and Molecular Biology, University of Bochum, D- 44780 Bochum, Germany.
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