Evidence map›Paper›PMID 29548275›Full record

ArticleBMC plant biology2018

OsNOA1 functions in a threshold-dependent manner to regulate chloroplast proteins in rice at lower temperatures.

Han He, Qiaosong Yang, Boran Shen, Sheng Zhang, Xinxiang Peng

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.6field-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

4 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Nitrate Reductase-Mediated Nitric Oxide Regulates the Leaf Shape inInternational journal of molecular sciences · 2019
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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 3 institutions in 2 countries.

Han HeState Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, South China Agricultural University, Guangzhou, China.
Qiaosong YangInstitute of Fruit Tree Research, Guangdong Academy of Agricultural Sciences, Guangzhou, China.
Boran ShenState Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, South China Agricultural University, Guangzhou, China.
Sheng ZhangInstitute of Biotechnology, Cornell University, Ithaca, USA.
Xinxiang PengState Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, South China Agricultural University, Guangzhou, China. xpeng@scau.edu.cn.
South China Agricultural University · CNCornell University · USGuangdong Academy of Agricultural Sciences · CN

Funding

National Natural Science Foundation of China 31170222Science and Technology Planning of Guangzhou City 201607020006
6 · The paper itself

Abstract

backgroundAlthough decreased protein expressions have been observed in NOA1 (Nitric Oxide Associated protein 1) deficient plants, the molecular mechanisms of how NOA1 regulates protein metabolism remain poorly understood. In this study, we have used a global comparative proteomic approach for both OsNOA1 suppression and overexpression transgenic lines under two different temperatures, in combination with physiological and biochemical analyses to explore the regulatory mechanisms of OsNOA1 in rice.

resultsIn OsNOA1-silenced or highly overexpressed rice, considerably different expression patterns of both chlorophyll and Rubisco as well as distinct phenotypes were observed between the growth temperatures at 22 °C and 30 °C. These observations led us to hypothesize there appears a narrow abundance threshold for OsNOA1 to function properly at lower temperatures, while higher temperatures seem to partially compensate for the changes of OsNOA1 abundance. Quantitative proteomic analyses revealed higher temperatures could restore 90% of the suppressed proteins to normal levels, whereas almost all of the remaining suppressed proteins were chloroplast ribosomal proteins. Additionally, our data showed 90% of the suppressed proteins in both types of transgenic plants at lower temperatures were located in the chloroplast, suggesting a primary effect of OsNOA1 on chloroplast proteins. Transcript analyses, along with in vitro pull-down experiments further demonstrated OsNOA1 is associated with the function of chloroplast ribosomes.

conclusionsOur results suggest OsNOA1 functions in a threshold-dependent manner for regulation of chloroplast proteins at lower temperatures, which may be mediated by interactions between OsNOA1 and chloroplast ribosomes.

Indexed as

ChlorophyllChloroplastsGene Expression Regulation, PlantOryzaPlant ProteinsPlants, Genetically ModifiedProteomicsRibulose-Bisphosphate CarboxylaseTemperatureChlorophyllPlant ProteinsRibulose-Bisphosphate CarboxylaseChloroplastNOA1Quantitative proteomicsRiceTandem mass tagThreshold-dependent

Identifiers

PMID29548275
PMCPMC5857130
OpenAlexW2790717870

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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.