ArticleNucleic acids research2002
Endonucleolytic activation directs dark-induced chloroplast mRNA degradation.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- NewAntioxidants (Basel, Switzerland) · 2022Article
- Interaction of 2',3'-cAMP with Rbp47b Plays a Role in Stress Granule Formation.Plant physiology · 2018Article
- Wheat proteomics: proteome modulation and abiotic stress acclimation.Frontiers in plant science · 2014Review
- Changes in physiology and protein abundance in salt-stressed wheat chloroplasts.Molecular biology reports · 2012Article
- Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks.Plant physiology · 2009Article
- Arabidopsis thaliana mutants reveal a role for CSP41a and CSP41b, two ribosome-associated endonucleases, in chloroplast ribosomal RNA metabolism.Plant molecular biology · 2008Article
- Dark-induced mRNA instability involves RNase E/G-type endoribonuclease cleavage at the AU-box and SD sequences in cyanobacteria.Molecular genetics and genomics : MGG · 2007Article
- Mammalian polynucleotide phosphorylase is an intermembrane space RNase that maintains mitochondrial homeostasis.Molecular and cellular biology · 2006Article
- A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space.Molecular and cellular biology · 2006Article
- ABA-responsive RNA-binding proteins are involved in chloroplast and stromule function in Arabidopsis seedlings.Planta · 2006Article
- The Fed-1 (CAUU)4 element is a 5' UTR dark-responsive mRNA instability element that functions independently of dark-induced polyribosome dissociation.Plant molecular biology · 2004Article
- Proteomics gives insight into the regulatory function of chloroplast thioredoxins.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 stem-loop 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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