Evidence map›Paper›PMID 19666611›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Cysteine modification of a specific repressor protein controls the translational status of nucleus-encoded LHCII mRNAs in Chlamydomonas.

Lutz Wobbe, Olga Blifernez, Christian Schwarz, Jan H Mussgnug, Jörg Nickelsen, Olaf Kruse

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 59 citations in OpenAlex.

  1. Can thiol-based redox systems be utilized as parts for synthetic biology applications?Redox report : communications in free radical research · 2021
    Article
  2. COPlant, cell & environment · 2021
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  14. Thiol-based redox switches and gene regulation.Antioxidants & redox signaling · 2011
    Review
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  16. Interplay between COPhysiologia plantarum
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Lutz WobbeDepartment of Biology, University of Bielefeld, Algae BioTech Group, Universitätsstrasse 25, D-33615 Bielefeld, Germany.
Olga Blifernez
Christian Schwarz
Jan H Mussgnug
Jörg Nickelsen
Olaf Kruse
Bielefeld University · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cytosolic RNA-binding protein NAB1 represses translation of LHCII (light-harvesting complex of photosystem II) encoding mRNAs by sequestration into translationally silent mRNP complexes in the green alga Chlamydomonas reinhardtii. NAB1 contains 2 cysteine residues, Cys-181 and Cys-226, within its C-terminal RRM motif. Modification of these cysteines either by oxidation or by alkylation in vitro was accompanied by a decrease in RNA-binding affinity for the target mRNA sequence. To confirm the relevance of reversible NAB1 cysteine oxidation for the regulation of its activity in vivo, we replaced both cysteines with serines. All examined cysteine single and double mutants exhibited a reduced antenna at PSII caused by a perturbed NAB1 deactivation mechanism, with double mutations and Cys-226 single mutations causing a stronger and more distinctive phenotype compared with the Cys-181 mutation. Our data indicated that the responsible redox control mechanism is mediated by modification of single cysteines. Polysome analyses and RNA co-immunoprecipitation experiments demonstrated the interconnection of the NAB1 thiol state and its activity as a translation repressor in vivo. NAB1 is fully active in its dithiol state and is reversibly deactivated by modification of its cysteines. In summary, this work is an example that cytosolic translation of nucleus encoded photosynthetic genes is regulated via a reversible cysteine-based redox switch in a RNA-binding translation repressor protein.

Indexed as

Protein BiosynthesisAlgal ProteinsAmino Acid SubstitutionAnimalsCell NucleusChlamydomonas reinhardtiiCysteineDown-RegulationLightMutationOxidative StressPhenotypePhotosystem II Protein ComplexPhototrophic ProcessesProtein BindingProtein StabilityAlgal ProteinsCysteinePhotosystem II Protein ComplexRepressor ProteinsRNA, AlgalRNA, MessengerSerine

Identifiers

PMID19666611
PMCPMC2726419
OpenAlexW1964453365

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.