Evidence map›Paper›PMID 29581280›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis.

Peng Wang, Fu-Cheng Liang, Daniel Wittmann, Alex Siegel, Shu-Ou Shan, Bernhard Grimm

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 69 citations in OpenAlex.

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  5. Proteome and Metabolome Analyses of Albino Bracts inPlants (Basel, Switzerland) · 2025
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  7. Article
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  13. An ankyrin repeat chaperone targets toxic oligomers during amyloidogenesis.Protein science : a publication of the Protein Society · 2023
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  16. Review
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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

6 authors at 2 institutions in 2 countries.

Peng WangDepartment of Plant Physiology, Institute of Biology, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.
Fu-Cheng LiangDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.
Daniel WittmannDepartment of Plant Physiology, Institute of Biology, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.
Alex SiegelDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.
Shu-Ou ShanDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.ORCID 0000-0002-6526-1733
Bernhard GrimmDepartment of Plant Physiology, Institute of Biology, Humboldt-Universität zu Berlin, 10115 Berlin, Germany; bernhard.grimm@rz.hu-berlin.de.
California Institute of Technology · USHumboldt-Universität zu Berlin · DE

Funding

Understanding Molecular Chaperones during Membrane Protein BiogenesisR01GM114390 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI SHAN, SHU-OU · 2016 to 2019
$1.4M
NIGMS NIH HHS R01 GM114390
6 · The paper itself

Abstract

Assembly of light-harvesting complexes requires synchronization of chlorophyll (Chl) biosynthesis with biogenesis of light-harvesting Chl a/b-binding proteins (LHCPs). The chloroplast signal recognition particle (cpSRP) pathway is responsible for transport of nucleus-encoded LHCPs in the stroma of the plastid and their integration into the thylakoid membranes. Correct folding and assembly of LHCPs require the incorporation of Chls, whose biosynthesis must therefore be precisely coordinated with membrane insertion of LHCPs. How the spatiotemporal coordination between the cpSRP machinery and Chl biosynthesis is achieved is poorly understood. In this work, we demonstrate a direct interaction between cpSRP43, the chaperone that mediates LHCP targeting and insertion, and glutamyl-tRNA reductase (GluTR), a rate-limiting enzyme in tetrapyrrole biosynthesis. Concurrent deficiency for cpSRP43 and the GluTR-binding protein (GBP) additively reduces GluTR levels, indicating that cpSRP43 and GBP act nonredundantly to stabilize GluTR. The substrate-binding domain of cpSRP43 binds to the N-terminal region of GluTR, which harbors aggregation-prone motifs, and the chaperone activity of cpSRP43 efficiently prevents aggregation of these regions. Our work thus reveals a function of cpSRP43 in Chl biosynthesis and suggests a striking mechanism for posttranslational coordination of LHCP insertion with Chl biosynthesis.

Indexed as

Aldehyde OxidoreductasesArabidopsisArabidopsis ProteinsChlorophyllChloroplast ProteinsChloroplastsLight-Harvesting Protein ComplexesMolecular ChaperonesProtein BindingProtein FoldingProtein TransportSignal Recognition ParticleTetrapyrrolesAldehyde OxidoreductasesArabidopsis ProteinsChlorophyllChloroplast ProteinscpSRP43 protein, Arabidopsisglutamyl tRNA reductaseLight-Harvesting Protein ComplexesMolecular ChaperonesSignal Recognition ParticleTetrapyrroles5-aminolevulinic acidchaperonechloroplast biogenesischloroplast signal recognition particletetrapyrrole biosynthesis

Identifiers

PMID29581280
PMCPMC5899456
OpenAlexW2790071334

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.