Evidence map›Paper›PMID 19117946›Full record

ArticleThe Journal of biological chemistry2009

Flexibility in anaerobic metabolism as revealed in a mutant of Chlamydomonas reinhardtii lacking hydrogenase activity.

Alexandra Dubini, Florence Mus, Michael Seibert, Arthur R Grossman, Matthew C Posewitz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 106 citations in OpenAlex.

  1. Review
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  3. Three genomes in the algal genusProceedings of the National Academy of Sciences of the United States of America · 2021
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  4. Water oxidation by photosystem II is the primary source of electrons for sustained HProceedings of the National Academy of Sciences of the United States of America · 2020
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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

5 authors at 3 institutions in 1 country.

Alexandra DubiniEnvironmental Science and Engineering Division, Colorado School of Mines, Golden, Colorado 80401, USA.
Florence Mus
Michael Seibert
Arthur R Grossman
Matthew C Posewitz
Department of Plant Biology · USNational Renewable Energy Laboratory · USColorado School of Mines · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The green alga Chlamydomonas reinhardtii has a network of fermentation pathways that become active when cells acclimate to anoxia. Hydrogenase activity is an important component of this metabolism, and we have compared metabolic and regulatory responses that accompany anaerobiosis in wild-type C. reinhardtii cells and a null mutant strain for the HYDEF gene (hydEF-1 mutant), which encodes an [FeFe] hydrogenase maturation protein. This mutant has no hydrogenase activity and exhibits elevated accumulation of succinate and diminished production of CO2 relative to the parental strain during dark, anaerobic metabolism. In the absence of hydrogenase activity, increased succinate accumulation suggests that the cells activate alternative pathways for pyruvate metabolism, which contribute to NAD(P)H reoxidation, and continued glycolysis and fermentation in the absence of O2. Fermentative succinate production potentially proceeds via the formation of malate, and increases in the abundance of mRNAs encoding two malate-forming enzymes, pyruvate carboxylase and malic enzyme, are observed in the mutant relative to the parental strain following transfer of cells from oxic to anoxic conditions. Although C. reinhardtii has a single gene encoding pyruvate carboxylase, it has six genes encoding putative malic enzymes. Only one of the malic enzyme genes, MME4, shows a dramatic increase in expression (mRNA abundance) in the hydEF-1 mutant during anaerobiosis. Furthermore, there are marked increases in transcripts encoding fumarase and fumarate reductase, enzymes putatively required to convert malate to succinate. These results illustrate the marked metabolic flexibility of C. reinhardtii and contribute to the development of an informed model of anaerobic metabolism in this and potentially other algae.

Indexed as

Algal ProteinsAnaerobiosisAnimalsCarbon DioxideChlamydomonas reinhardtiiEndopeptidasesHydrogenaseMalate DehydrogenaseMutationNADPOxidation-ReductionProtozoan ProteinsPyruvic AcidSuccinate DehydrogenaseSuccinic AcidAlgal ProteinsCarbon DioxideEndopeptidasesHydrogenasehydrogenase maturating endopeptidase HYBDMalate DehydrogenaseNADPProtozoan ProteinsPyruvic AcidSuccinate DehydrogenaseSuccinic Acid

Identifiers

PMID19117946
PMCPMC2652310
OpenAlexW1988339395

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.