Evidence map›Paper›PMID 37714932›Full record

ArticleCommunications biology2023

Identification of a c-type heme oxygenase and its function during acclimation of cyanobacteria to nitrogen fluctuations.

Zhaoxing Ran, Zhenyu Du, Gengkai Miao, Mei Zheng, Ligang Luo, Xiaoqin Pang, Lanzhen Wei, Dezhi Li, Weimin Ma

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. 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
1.7field-weighted citation impact, top 17% 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, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
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

9 authors at 2 institutions in 3 countries.

Zhaoxing RanSchool of Ecological and Environmental Sciences, East China Normal University, 200241, Shanghai, China.ORCID http://orcid.org/0000-0001-6320-3487
Zhenyu DuCollege of Life Sciences, Shanghai Normal University, 200234, Shanghai, China.
Gengkai MiaoCollege of Life Sciences, Shanghai Normal University, 200234, Shanghai, China.
Mei ZhengCollege of Life Sciences, Shanghai Normal University, 200234, Shanghai, China.
Ligang LuoCollege of Life Sciences, Shanghai Normal University, 200234, Shanghai, China.
Xiaoqin PangCollege of Life Sciences, Shanghai Normal University, 200234, Shanghai, China.
Lanzhen WeiCollege of Life Sciences, Shanghai Normal University, 200234, Shanghai, China. weilz@shnu.edu.cn.ORCID http://orcid.org/0009-0009-4628-1534
Dezhi LiSchool of Ecological and Environmental Sciences, East China Normal University, 200241, Shanghai, China. dzli@des.ecnu.edu.cn.ORCID http://orcid.org/0000-0002-8482-2372
Weimin MaCollege of Life Sciences, Shanghai Normal University, 200234, Shanghai, China. wma@shnu.edu.cn.ORCID http://orcid.org/0000-0003-4964-415X
Shanghai Normal University · CNNew York University Shanghai · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanisms of acclimating to a nitrogen-fluctuating environment are necessary for the survival of aquatic cyanobacteria in their natural habitats, but our understanding is still far from complete. Here, the synthesis of phycobiliprotein is confirmed to be much earlier than that of photosystem components during recovery from nitrogen chlorosis and an unknown protein Ssr1698 is discovered to be involved in this synthetic process. The unknown protein is further identified as a c-type heme oxygenase (cHO) in tetrapyrrole biosynthetic pathway and catalyzes the opening of heme ring to form biliverdin IXα, which is required for phycobilin production and ensuing phycobiliprotein synthesis. In addition, the cHO-dependent phycobiliprotein is found to be vital for the growth of cyanobacterial cells during chlorosis and regreening through its nitrogen-storage and light-harvesting functions, respectively. Collectively, the cHO expressed preferentially during recovery from nitrogen chlorosis is identified in photosynthetic organisms and the dual function of this enzyme-dependent phycobiliprotein is proposed to be an important mechanism for acclimation of aquatic cyanobacteria to a nitrogen-fluctuating environment.

Indexed as

Anemia, HypochromicCyanobacteriaAcclimatizationHeme Oxygenase (Decyclizing)HumansNitrogenPhycobiliproteinsHeme Oxygenase (Decyclizing)NitrogenPhycobiliproteins

Identifiers

PMID37714932
PMCPMC10504260
OpenAlexW4386769018

What OpenQuestion holds

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LicenceCC BY
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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.