Evidence map›Paper›PMID 27585744›Full record

ArticleScientific reports2016

A Nucleus-Encoded Chloroplast Protein YL1 Is Involved in Chloroplast Development and Efficient Biogenesis of Chloroplast ATP Synthase in Rice.

Fei Chen, Guojun Dong, Limin Wu, Fang Wang, Xingzheng Yang, Xiaohui Ma, Haili Wang, Jiahuan Wu, Yanli Zhang, Huizhong Wang and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 30 citations in OpenAlex.

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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

12 authors at 3 institutions in 1 country.

Fei ChenCollege of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Guojun DongState Key Laboratory for Rice Biology, China National Rice Research Institute, Hangzhou 310006, Zhejiang, China.
Limin WuCollege of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Fang WangInstitute of Insect Sciences, Zhejiang University, Hangzhou 310058, China.
Xingzheng YangCollege of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Xiaohui MaCollege of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Haili WangCollege of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Jiahuan WuCollege of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Yanli ZhangCollege of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Huizhong WangCollege of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Qian QianState Key Laboratory for Rice Biology, China National Rice Research Institute, Hangzhou 310006, Zhejiang, China.
Yanchun YuCollege of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 310036, China.
Hangzhou Normal University · CNChina National Rice Research Institute · CNZhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplast ATP synthase (cpATPase) is an importance thylakoid membrane-associated photosynthetic complex involved in the light-dependent reactions of photosynthesis. In this study, we isolated and characterized a rice (Oryza sativa) mutant yellow leaf 1 (yl1), which exhibits chlorotic leaves throughout developmental stages. The YL1 mutation showed reduced chlorophyll contents, abnormal chloroplast morphology, and decreased photochemical efficiency. Moreover, YL1 deficiency disrupts the expression of genes associated with chloroplast development and photosynthesis. Molecular and genetic analyses revealed that YL1 is a nucleus-encoded protein with a predicted transmembrane domain in its carboxyl-terminus that is conserved in the higher plant kingdom. YL1 localizes to chloroplasts and is preferentially expressed in green tissues containing chloroplasts. Immunoblot analyses showed that inactivation of YL1 leads to drastically reduced accumulation of AtpA (α) and AtpB (β), two core subunits of CF1αβ subcomplex of cpATPase, meanwhile, a severe decrease (ca. 41.7%) in cpATPase activity was observed in the yl1-1 mutant compared with the wild type. Furthermore, yeast two-hybrid and bimolecular fluorescence complementation assays revealed a specific interaction between YL1 and AtpB subunit of cpATPase. Taken together, our results suggest that YL1 is a plant lineage-specific auxiliary factor involved in the biogenesis of the cpATPase complex, possibly via interacting with the β-subunit.

Indexed as

Cell NucleusChloroplast ProteinsChloroplast Proton-Translocating ATPasesChloroplastsGene Expression Regulation, PlantImmunoblottingMicroscopy, Electron, TransmissionMutationOryzaPhotosynthesisPlant LeavesProtein BindingChloroplast ProteinsChloroplast Proton-Translocating ATPases

Identifiers

PMID27585744
PMCPMC5009372
OpenAlexW2512844302

What OpenQuestion holds

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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.