Evidence map›Paper›PMID 35064202›Full record

ArticleCommunications biology2022

NapB Restores cytochrome c biosynthesis in bacterial dsbD-deficient mutants.

Kailun Guo, Xue Feng, Weining Sun, Sirui Han, Shihua Wu, Haichun Gao

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  8. A novel bacterial sulfite dehydrogenase that requires threeApplied and environmental microbiology · 2023
    Article
  9. Article
  10. Pleiotropic Effects of Hfq on the CytochromeApplied and environmental microbiology · 2022
    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

6 authors at 2 institutions in 1 country.

Kailun Guo *Institute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, China.
Xue Feng *Institute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, China.
Weining SunInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, China.
Sirui HanInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, China.
Shihua WuInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, China. drwushihua@zju.edu.cn.ORCID 0000-0002-1669-7522
Haichun GaoInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, China. haichung@zju.edu.cn.ORCID 0000-0002-2647-6563
Zhejiang University · CNZhejiang University-University of Edinburgh Institute · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochromes c (cyts c), essential for respiration and photosynthesis in eukaryotes, confer bacteria respiratory versatility for survival and growth in natural environments. In bacteria having a cyt c maturation (CCM) system, DsbD is required to mediate electron transport from the cytoplasm to CcmG of the Ccm apparatus. Here with cyt c-rich Shewanella oneidensis as the research model, we identify NapB, a cyt c per se, that suppresses the CCM defect of a dsbD mutant during anaerobiosis, when NapB is produced at elevated levels, a result of activation by cAMP-Crp. Data are then presented to suggest that NapB reduces CcmG, leading to the suppression. We further show that NapB proteins capable of rescuing CCM in the dsbD mutant form a small distinct clade. The study sheds light on multifunctionality of cyts c, and more importantly, unravels a self-salvation strategy through which bacteria have evolved to better adjust to the natural world.

Indexed as

Bacterial ProteinsCytochromes cGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicModels, MolecularMutationOxidoreductasesProtein ConformationProtein IsoformsShewanellaBacterial ProteinsCytochromes cOxidoreductasesProtein Isoforms

Identifiers

PMID35064202
PMCPMC8782879
OpenAlexW4205849315

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.