Nucleic Acids Research, 2002, Vol. 30, No. 20 4527-4533
© 2002 Oxford University Press
Endonucleolytic activation directs dark-induced chloroplast mRNA degradation
Institute of Plant Sciences, Swiss Federal Institute of Technology, ETH Zentrum, LFW E51.1, Universitätstrasse 2, CH-8092 Zürich, Switzerland
*To whom correspondence should be addressed. Tel: +41 1 632 3866; Fax: +41 1 632 1079; Email: sacha.baginsky{at}ipw.biol.ethz.ch
Plastid mRNA stability is tightly regulated by external signals such as light. We have investigated the biochemical mechanism responsible for the dark-induced decrease of relative half-lives for mRNAs encoding photosynthetic proteins. Protein fractions isolated from plastids of light-grown and dark-adapted plants correctly reproduced an RNA degradation pathway in the dark that is downregulated in the light. This dark-dependent pathway is initiated by endonucleolytic cleavages in the petD mRNA precursor substrate proximal to a region that can fold into a stemloop structure. Polynucleotide phosphorylase (PNPase) polyadenylation activity was strongly increased in the protein fraction isolated from plastids in dark-adapted plants, but interestingly PNPase activity was not required for the initiation of dark-induced mRNA degradation. A protein factor present in the protein fraction from plastids of light-grown plants could inactivate the endonuclease activity and thereby stabilize the RNA substrate in the protein fraction from plastids of dark-adapted plants. The results show that plastid mRNA stability is effectively controlled by the regulation of a specific dark-induced RNA degradation pathway.
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