Evidence map›Paper›PMID 26511314›Full record

ArticleThe Journal of biological chemistry2015

In Vivo Studies in Rhodospirillum rubrum Indicate That Ribulose-1,5-bisphosphate Carboxylase/Oxygenase (Rubisco) Catalyzes Two Obligatorily Required and Physiologically Significant Reactions for Distinct Carbon and Sulfur Metabolic Pathways.

Swati Dey, Justin A North, Jaya Sriram, Bradley S Evans, F Robert Tabita

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
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  7. On a Possible Way to Increase the Efficiency of Photosynthesis.Doklady. Biochemistry and biophysics · 2020
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  8. Review
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  11. Article
  12. Microbial pathway for anaerobic 5'-methylthioadenosine metabolism coupled to ethylene formation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Article
  14. Article
  15. 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

5 authors at 2 institutions in 1 country.

Swati DeyFrom the Department of Microbiology, The Ohio State University, Columbus, Ohio 43210 and.
Justin A NorthFrom the Department of Microbiology, The Ohio State University, Columbus, Ohio 43210 and.
Jaya SriramFrom the Department of Microbiology, The Ohio State University, Columbus, Ohio 43210 and.
Bradley S Evansthe Donald Danforth Plant Science Center, St. Louis, Missouri, 63132.
F Robert TabitaFrom the Department of Microbiology, The Ohio State University, Columbus, Ohio 43210 and tabita.1@osu.edu.ORCID http://orcid.org/0000-0001-7338-447X
The Ohio State University · USDonald Danforth Plant Science Center · US

Funding

One Enzyme for Two Distinct MetabolismsR01GM095742 · NIGMS · OHIO STATE UNIVERSITY · PI TABITA, F ROBERT · 2011 to 2014
$1.1M
Characterization of novel sulfur salvage mechanisms in Rodospirillum rubrumF32GM109547 · NIGMS · OHIO STATE UNIVERSITY · PI NORTH, JUSTIN ANDREW · 2014 to 2015
$112k
NIGMS NIH HHS F32 GM109547NIGMS NIH HHS F32GM109547NIGMS NIH HHS GM095742NIGMS NIH HHS R01 GM095742
6 · The paper itself

Abstract

All organisms possess fundamental metabolic pathways to ensure that needed carbon and sulfur compounds are provided to the cell in the proper chemical form and oxidation state. For most organisms capable of using CO2 as sole source of carbon, ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) catalyzes primary carbon dioxide assimilation. In addition, sulfur salvage pathways are necessary to ensure that key sulfur-containing compounds are both available and, where necessary, detoxified in the cell. Using knock-out mutations and metabolomics in the bacterium Rhodospirillum rubrum, we show here that Rubisco concurrently catalyzes key and essential reactions for seemingly unrelated but physiologically essential central carbon and sulfur salvage metabolic pathways of the cell. In this study, complementation and mutagenesis studies indicated that representatives of all known extant functional Rubisco forms found in nature are capable of simultaneously catalyzing reactions required for both CO2-dependent growth as well as growth using 5-methylthioadenosine as sole sulfur source under anaerobic photosynthetic conditions. Moreover, specific inactivation of the CO2 fixation reaction did not affect the ability of Rubisco to support anaerobic 5-methylthioadenosine metabolism, suggesting that the active site of Rubisco has evolved to ensure that this enzyme maintains both key functions. Thus, despite the coevolution of both functions, the active site of this protein may be differentially modified to affect only one of its key functions.

Indexed as

Metabolic Networks and PathwaysBacterial ProteinsBiocatalysisCarbonCarbon DioxideDeoxyadenosinesRhodospirillum rubrumRibulose-Bisphosphate CarboxylaseSulfurThionucleosides5'-methylthioadenosineBacterial ProteinsCarbonCarbon DioxideDeoxyadenosinesRibulose-Bisphosphate CarboxylaseSulfurThionucleosides5-methylthioadenosinecarbon fixationenzymemetabolismmetabololomicsmetabolomicsmethylthioadenosineribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO)sulfursulfur salvage

Identifiers

PMID26511314
PMCPMC4692197
OpenAlexW2212477841

What OpenQuestion holds

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Registered trials

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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.