Evidence map›Paper›PMID 27208236›Full record

ArticlePlant physiology2016

Functional Characterization of the Subunits N, H, J, and O of the NAD(P)H Dehydrogenase Complexes in Synechocystis sp. Strain PCC 6803.

Zhihui He, Hualing Mi

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  6. Proteomic analysis of unicellular cyanobacteriumbioRxiv : the preprint server for biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Cyanobacterial NDH-1 Complexes.Frontiers in microbiology · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Complete Chloroplast Genome ofPlants (Basel, Switzerland) · 2020
    Article
  15. Article
  16. 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

2 authors at 1 institution in 1 country.

Zhihui HeNational Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Science, Shanghai 200032, China.ORCID 0000-0003-4184-8377
Hualing MiNational Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Science, Shanghai 200032, China mihl@sippe.ac.cn.ORCID 0000-0003-1021-8372
Center for Excellence in Molecular Plant Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cyanobacterial NAD(P)H dehydrogenase (NDH-1) complexes play crucial roles in variety of bioenergetic reactions such as respiration, CO2 uptake, and cyclic electron transport around PSI. Recently, substantial progress has been made in identifying the composition of subunits of NDH-1 complexes. However, the localization and the physiological roles of several subunits in cyanobacteria are not fully understood. Here, by constructing fully segregated ndhN, ndhO, ndhH, and ndhJ null mutants in Synechocystis sp. strain PCC 6803, we found that deletion of ndhN, ndhH, or ndhJ but not ndhO severely impaired the accumulation of the hydrophilic subunits of the NDH-1 in the thylakoid membrane, resulting in disassembly of NDH-1MS, NDH-1MS', as well as NDH-1L, finally causing the severe growth suppression phenotype. In contrast, deletion of NdhO affected the growth at pH 6.5 in air. In the cytoplasm, either NdhH or NdhJ deleted mutant, but neither NdhN nor NdhO deleted mutant, failed to accumulate the NDH-1 assembly intermediate consisting of NdhH, NdhJ, NdhK, and NdhM. Based on these results, we suggest that NdhN, NdhH, and NdhJ are essential for the stability and the activities of NDH-1 complexes, while NdhO for NDH-1 functions under the condition of inorganic carbon limitation in Synechocystis sp. strain PCC 6803. We discuss the roles of these subunits and propose a new NDH-1 model.

Indexed as

AirCytoplasmGene DeletionHeterotrophic ProcessesLightModels, BiologicalMultienzyme ComplexesNADPH DehydrogenasePhenotypeProtein BindingProtein SubunitsReproducibility of ResultsSynechocystisMultienzyme ComplexesNADPH DehydrogenaseProtein Subunits

Identifiers

PMID27208236
PMCPMC4902626
OpenAlexW2337387404

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.