Evidence map›Paper›PMID 24847053›Full record

ArticleThe Journal of biological chemistry2014

NdhP is an exclusive subunit of large complex of NADPH dehydrogenase essential to stabilize the complex in Synechocystis sp. strain PCC 6803.

Jingsong Zhang, Fudan Gao, Jiaohong Zhao, Teruo Ogawa, Quanxi Wang, Weimin Ma

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

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  8. Review
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  10. Molecular dynamics and structural models of the cyanobacterial NDH-1 complex.Biochimica et biophysica acta. Bioenergetics · 2019
    Article
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  12. NDH-1 Is Important for Photosystem I Function ofFrontiers in plant science · 2017
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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.

Jingsong ZhangFrom the College of Life and Environment Sciences, Shanghai Normal University, Guilin Road 100, Shanghai 200234, China and.
Fudan GaoFrom the College of Life and Environment Sciences, Shanghai Normal University, Guilin Road 100, Shanghai 200234, China and.
Jiaohong ZhaoFrom the College of Life and Environment Sciences, Shanghai Normal University, Guilin Road 100, Shanghai 200234, China and.
Teruo Ogawathe Bioscience Center, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
Quanxi WangFrom the College of Life and Environment Sciences, Shanghai Normal University, Guilin Road 100, Shanghai 200234, China and.
Weimin MaFrom the College of Life and Environment Sciences, Shanghai Normal University, Guilin Road 100, Shanghai 200234, China and wma@shnu.edu.cn cyanoma@hotmail.com.
Shanghai Normal University · CNNagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two major complexes of NADPH dehydrogenase (NDH-1) have been identified in cyanobacteria. A large complex (NDH-1L) contains NdhD1 and NdhF1, which are absent in a medium size complex (NDH-1M). They play important roles in respiration, cyclic electron transport around photosystem I, and CO2 acquisition. Two mutants sensitive to high light for growth and impaired in NDH-1-mediated cyclic electron transfer were isolated from Synechocystis sp. strain PCC 6803 transformed with a transposon-bearing library. Both mutants had a tag in sml0013 encoding NdhP, a single transmembrane small subunit of the NDH-1 complex. During prolonged incubation of the wild type thylakoid membrane with n-dodecyl β-d-maltoside (DM), about half of the NDH-1L was disassembled to NDH-1M and the rest decomposed completely without forming NDH-1M. In the ndhP deletion mutant (ΔndhP), disassembling of NDH-1L to NDH-1M occurred even on ice, and decomposition to a small piece occurred at room temperature much faster than in the wild type. Deletion of the C-terminal tail of NdhP gave the same result. The C terminus of NdhP was tagged by YFP-His6. Blue native gel electrophoresis of the DM-treated thylakoid membrane of this strain and Western analysis using the antibody against GFP revealed that NdhP-YFP-His6 was exclusively confined to NDH-1L. During prolonged incubation of the thylakoid membrane of the tagged strain with DM at room temperature, NDH-1L was partially disassembled to NDH-1M and the 160-kDa band containing NdhP-YFP-His6 and possibly NdhD1 and NdhF1. We therefore conclude that NdhP, especially its C-terminal tail, is essential to assemble NdhD1 and NdhF1 and stabilize the NDH-1L complex.

Indexed as

Amino Acid SequenceCell RespirationElectron TransportEnzyme StabilityMolecular Sequence DataNADPH DehydrogenasePhotosystem I Protein ComplexProtein SubunitsProtein TransportSequence DeletionSynechocystisNADPH DehydrogenasePhotosystem I Protein ComplexProtein SubunitsCyanobacteriaElectron Transfer ComplexMembrane EnzymeMutantNDH-1L ComplexNDH-CETNdhPPhotosynthesisStabilizationSynechocystis 6803

Identifiers

PMID24847053
PMCPMC4081920
OpenAlexW2009819840

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.