Evidence map›Paper›PMID 31925322›Full record

ArticleCommunications biology2020

An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase.

Iskander M Ibrahim, Huan Wu, Roman Ezhov, Gilbert E Kayanja, Stanislav D Zakharov, Yanyan Du, Weiguo Andy Tao, Yulia Pushkar, William A Cramer, Sujith Puthiyaveetil

Abstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Identification and characterization ofHorticulture research · 2026
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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

10 authors.

Iskander M IbrahimDepartment of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.ORCID http://orcid.org/0000-0002-2744-6307
Huan WuDepartment of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.
Roman EzhovDepartment of Physics and Astronomy, Purdue University, 525 Northwestern Avenue, West Lafayette, IN, 47907, USA.
Gilbert E KayanjaDepartment of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.
Stanislav D ZakharovDepartment of Biological Sciences, Purdue University, West Lafayette, IN, 47907, USA.
Yanyan DuDepartment of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.
Weiguo Andy TaoDepartment of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA.
Yulia PushkarDepartment of Physics and Astronomy, Purdue University, 525 Northwestern Avenue, West Lafayette, IN, 47907, USA.
William A CramerDepartment of Biological Sciences, Purdue University, West Lafayette, IN, 47907, USA.
Sujith PuthiyaveetilDepartment of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA. spveetil@purdue.edu.ORCID http://orcid.org/0000-0001-7505-4511

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic efficiency depends on equal light energy conversion by two spectrally distinct, serially-connected photosystems. The redox state of the plastoquinone pool, located between the two photosystems, is a key regulatory signal that initiates acclimatory changes in the relative abundance of photosystems. The Chloroplast Sensor Kinase (CSK) links the plastoquinone redox signal with photosystem gene expression but the mechanism by which it monitors the plastoquinone redox state is unclear. Here we show that the purified Arabidopsis and Phaeodactylum CSK and the cyanobacterial CSK homologue, Histidine kinase 2 (Hik2), are iron-sulfur proteins. The Fe-S cluster of CSK is further revealed to be a high potential redox-responsive [3Fe-4S] center. CSK responds to redox agents with reduced plastoquinone suppressing its autokinase activity. Redox changes within the CSK iron-sulfur cluster translate into conformational changes in the protein fold. These results provide key insights into redox signal perception and propagation by the CSK-based chloroplast two-component system.

Indexed as

Oxidation-ReductionArabidopsis ProteinsChloroplastsEnzyme ActivationHistidine KinaseIronPhotosynthesisProtein ConformationRecombinant ProteinsSpectrum AnalysisStructure-Activity RelationshipSulfurArabidopsis Proteinschloroplast sensor kinase, ArabidopsisHistidine KinaseIronRecombinant ProteinsSulfur

Identifiers

PMID31925322
PMCPMC6949291

What OpenQuestion holds

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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.