ArticlePlant molecular biology2002
Light activates binding of membrane proteins to chloroplast RNAs in Chlamydomonas reinhardtii.
Article in Plant molecular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Biogenic membranes of the chloroplast in Chlamydomonas reinhardtii.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The nucleus-encoded trans-acting factor MCA1 plays a critical role in the regulation of cytochrome f synthesis in Chlamydomonas chloroplasts.The Plant cell · 2011Article
- Chloroplast protein targeting involves localized translation in Chlamydomonas.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Photosystem II assembly and repair are differentially localized in Chlamydomonas.The Plant cell · 2007Article
- Chloroplast RNA-binding proteins.Current genetics · 2003Review
- Mutagenesis of a light-regulated psbA intron reveals the importance of efficient splicing for photosynthetic growth.Nucleic acids research · 2003Article
- Chloroplast translation regulation.Photosynthesis researchReview
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several membrane proteins were previously shown to bind to the 5' leader of the chloroplast psbC mRNA in the unicellular eukaryotic alga Chlamydomonas reinhardtii. This study showed that these proteins have affinity for AU-rich RNAs, as determined by competition experiments. In addition, their binding activities are enhanced 13-15-fold by light, and a 46 kDa protein is activated within 1-10 min. This activation could be mediated by the modulation of ADP pools by the light-dependent reactions of photosynthesis and ATP synthase because (1) two inhibitors that block ATP synthesis also prevent this activation and (2) ADP inhibits the RNA-binding activity of this protein in vitro. An inhibitor of Photosystem II diminishes this induction, suggesting that reducing potential generated by the photosynthetic electron transport chain modulates this RNA-binding activity. The RNA-binding activities of two proteins (of 46 and 47 kDa) are inhibited by Mg-protoporphyrin IX methyl ester in vitro suggesting they could be regulated by these intermediates in the chlorophyll biosynthetic pathway.
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Registered trials
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