Evidence map›Paper›PMID 24610785›Full record

ArticleThe Journal of biological chemistry2014

Degradation of phycobilisomes in Synechocystis sp. PCC6803: evidence for essential formation of an NblA1/NblA2 heterodimer and its codegradation by A Clp protease complex.

Antje Baier, Wiebke Winkler, Thomas Korte, Wolfgang Lockau, Anne Karradt

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 67 citations in OpenAlex.

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  8. Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  16. Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

5 authors at 1 institution in 1 country.

Antje BaierInstitut für Biologie, Humboldt Universität zu Berlin, Chausseestrasse 117, D-10115 Berlin, Germany.
Wiebke WinklerInstitut für Biologie, Humboldt Universität zu Berlin, Chausseestrasse 117, D-10115 Berlin, Germany.
Thomas KorteGroup of Molecular Biophysics, Humboldt-Universität zu Berlin, Invalidenstrasse 42, D-10115 Berlin, Germany.
Wolfgang LockauInstitut für Biologie, Humboldt Universität zu Berlin, Chausseestrasse 117, D-10115 Berlin, Germany. Electronic address: wolfgang.lockau@biologie.hu-berlin.de.
Anne KarradtInstitut für Biologie, Humboldt Universität zu Berlin, Chausseestrasse 117, D-10115 Berlin, Germany.
Humboldt-Universität zu Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When cyanobacteria acclimate to nitrogen deficiency, they degrade their large (3-5-MDa), light-harvesting complexes, the phycobilisomes. This massive, yet specific, intracellular degradation of the pigmented phycobiliproteins causes a color change of cyanobacterial cultures from blue-green to yellow-green, a process referred to as chlorosis or bleaching. Phycobilisome degradation is induced by expression of the nblA gene, which encodes a protein of ~7 kDa. NblA most likely acts as an adaptor protein that guides a Clp protease to the phycobiliproteins, thereby initiating the degradation process. Most cyanobacteria and red algae possess just one nblA-homologous gene. As an exception, the widely used "model organism" Synechocystis sp. PCC6803 expresses two such genes, nblA16803 and nblA26803, both of whose products are required for phycobilisome degradation. Here, we demonstrate that the two NblA proteins heterodimerize in vitro and in vivo using pull-down assays and a Förster energy-transfer approach, respectively. We further show that the NblA proteins form a ternary complex with ClpC (the HSP100 chaperone partner of Clp proteases) and phycobiliproteins in vitro. This complex is susceptible to ATP-dependent degradation by a Clp protease, a finding that supports a proposed mechanism of the degradation process. Expression of the single nblA gene encoded by the genome of the N2-fixing, filamentous cyanobacterium Nostoc sp. PCC7120 in the nblA1/nblA2 mutant of Synechocystis sp. PCC6803 induced phycobilisome degradation, suggesting that the function of the NblA heterodimer of Synechocystis sp. PCC6803 is combined in the homodimeric protein of Nostoc sp. PCC7120.

Indexed as

Bacterial ProteinsDimerizationEndopeptidase ClpFluorescence Resonance Energy TransferPhycobilisomesProteolysisSynechocystisBacterial ProteinsEndopeptidase ClpPhycobilisomesCyanobacteriaFluorescence Resonance Energy Transfer (FRET)NblANitrogen StarvationPhycobilisome DegradationProteaseProtein DegradationProtein SynthesisSynechocystis

Identifiers

PMID24610785
PMCPMC4002084
OpenAlexW2033747530

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.