Evidence map›Paper›PMID 26941088›Full record

ArticleThe Plant cell2016

LIGHT-INDUCED RICE1 Regulates Light-Dependent Attachment of LEAF-TYPE FERREDOXIN-NADP+ OXIDOREDUCTASE to the Thylakoid Membrane in Rice and Arabidopsis.

Chao Yang, Hongtao Hu, Hongyan Ren, Yuzhu Kong, Hongwei Lin, Jiangfan Guo, Lingling Wang, Yi He, Xiaomeng Ding, Magda Grabsztunowicz and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 29 citations in OpenAlex.

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  15. Article
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  17. Article
  18. Article
  19. Review
  20. Association of Ferredoxin:NADPPhotosynthesis research · 2017
    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

18 authors at 3 institutions in 2 countries.

Chao YangState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Hongtao HuState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China National Engineering Technology Research Center for Slow and Controlled Release Fertilizers, Kingenta Ecological Engineering Group Co., Linyi, Shandong 276700, P.R. China.ORCID http://orcid.org/0000-0002-7323-2860
Hongyan RenCollege of Life Science, Shaanxi Normal University, Xi'an, Shaanxi Province 710062, P.R. China.ORCID http://orcid.org/0000-0002-4651-1047
Yuzhu KongState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.ORCID http://orcid.org/0000-0002-5271-051X
Hongwei LinState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Jiangfan GuoState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.ORCID http://orcid.org/0000-0001-6267-4260
Lingling WangState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Yi HeState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Xiaomeng DingState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Magda GrabsztunowiczMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20014 Turku, Finland.
Paula MuloMolecular Plant Biology, Department of Biochemistry, University of Turku, FI-20014 Turku, Finland.ORCID http://orcid.org/0000-0002-8728-3204
Tao ChenState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Yu LiuState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Zhongchang WuState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Yunrong WuState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Chuanzao MaoState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.ORCID http://orcid.org/0000-0001-5126-2180
Ping WuState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China.
Xiaorong MoState Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou 310058, P.R. China xiaorong@zju.edu.cn.
State Key Laboratory of Plant Physiology and BiochemistryUniversity of Turku · FIShaanxi Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LIR1 (LIGHT-INDUCED RICE1) encodes a 13-kD, chloroplast-targeted protein containing two nearly identical motifs of unknown function. LIR1 is present in the genomes of vascular plants, mosses, liverworts, and algae, but not in cyanobacteria. Using coimmunoprecipitation assays, pull-down assays, and yeast two-hybrid analyses, we showed that LIR1 interacts with LEAF-TYPE FERREDOXIN-NADP(+) OXIDOREDUCTASE (LFNR), an essential chloroplast enzyme functioning in the last step of photosynthetic linear electron transfer. LIR1 and LFNR formed high molecular weight thylakoid protein complexes with the TIC62 and TROL proteins, previously shown to anchor LFNR to the membrane. We further showed that LIR1 increases the affinity of LFNRs for TIC62 and that the rapid light-triggered degradation of the LIR1 coincides with the release of the LFNR from the thylakoid membrane. Loss of LIR1 resulted in a marked decrease in the accumulation of LFNR-containing thylakoid protein complexes without a concomitant decrease in total LFNR content. In rice (Oryza sativa), photosynthetic capacity of lir1 plants was slightly impaired, whereas no such effect was observed in Arabidopsis thaliana knockout mutants. The consequences of LIR1 deficiency in different species are discussed.

Indexed as

PhotosynthesisArabidopsisElectron TransportFerredoxin-NADP ReductaseFerredoxinsLightMultiprotein ComplexesMutationNADPOryzaPlant LeavesPlant ProteinsProteolysisSpecies SpecificityThylakoidsTwo-Hybrid System TechniquesFerredoxin-NADP ReductaseFerredoxinsMultiprotein ComplexesNADPPlant Proteins

Identifiers

PMID26941088
PMCPMC4826015
OpenAlexW2317508806

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.