Evidence map›Paper›PMID 27531955›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Thylakoid luminal θ-carbonic anhydrase critical for growth and photosynthesis in the marine diatom Phaeodactylum tricornutum.

Sae Kikutani, Kensuke Nakajima, Chikako Nagasato, Yoshinori Tsuji, Ai Miyatake, Yusuke Matsuda

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed, 1 pooled it
15.1field-weighted citation impact, top 1% 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

111 citing papers in PubMed, 1 synthesis or guideline pooled it, 266 citations in OpenAlex.

  1. Removal of pollutants from biogas slurry and COEnvironmental science and pollution research international · 2020
    Pooled it
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  18. Alpha Carbonic Anhydrase fromInternational journal of molecular sciences · 2024
    Article
  19. Article
  20. Algal chloroplast pyrenoids: Evidence for convergent evolution.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

51 more citing papers are in PubMed but not listed here.

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.

Sae KikutaniDepartment of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan;
Kensuke NakajimaDepartment of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan;
Chikako NagasatoMuroran Marine Station, Field Science Center for Northern Biosphere, Hokkaido University, Muroran, Hokkaido 051-0013, Japan.
Yoshinori TsujiDepartment of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan;
Ai MiyatakeDepartment of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan;
Yusuke MatsudaDepartment of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan; yusuke@kwansei.ac.jp.
Kwansei Gakuin University · JPHokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The algal pyrenoid is a large plastid body, where the majority of the CO2-fixing enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) resides, and it is proposed to be the hub of the algal CO2-concentrating mechanism (CCM) and CO2 fixation. The thylakoid membrane is often in close proximity to or penetrates the pyrenoid itself, implying there is a functional cooperation between the pyrenoid and thylakoid. Here, GFP tagging and immunolocalization analyses revealed that a previously unidentified protein, Pt43233, is targeted to the lumen of the pyrenoid-penetrating thylakoid in the marine diatom Phaeodactylum tricornutum The recombinant Pt43233 produced in Escherichia coli cells had both carbonic anhydrase (CA) and esterase activities. Furthermore, a Pt43233:GFP-fusion protein immunoprecipitated from P. tricornutum cells displayed a greater specific CA activity than detected for the purified recombinant protein. In an RNAi-generated Pt43233 knockdown mutant grown in atmospheric CO2 levels, photosynthetic dissolved inorganic carbon (DIC) affinity was decreased and growth was constantly retarded; in contrast, overexpression of Pt43233:GFP yielded a slightly greater photosynthetic DIC affinity. The discovery of a θ-type CA localized to the thylakoid lumen, with an essential role in photosynthetic efficiency and growth, strongly suggests the existence of a common role for the thylakoid-luminal CA with respect to the function of diverse algal pyrenoids.

Indexed as

Algal ProteinsAmino Acid SequenceCarbon CycleCarbon DioxideCarbonic AnhydrasesCloning, MolecularDiatomsEscherichia coliGene ExpressionGenetic VectorsKineticsPhotosynthesisRecombinant Fusion ProteinsRibulose-Bisphosphate CarboxylaseSequence AlignmentThylakoidsAlgal ProteinsCarbon DioxideCarbonic AnhydrasesRecombinant Fusion ProteinsRibulose-Bisphosphate CarboxylaseCGHR domainCO2-concentrating mechanismluminal carbonic anhydrasemarine diatompyrenoid

Identifiers

PMID27531955
PMCPMC5024579
OpenAlexW2508905367

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.