Evidence map›Paper›PMID 26283786›Full record

ArticleThe Journal of biological chemistry2015

Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase: product inhibition, cooperativity, and magnesium activation.

Suratna Hazra, J Nathan Henderson, Kevin Liles, Matthew T Hilton, Rebekka M Wachter

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 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
2.5field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

  1. Pooled it
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  3. Review
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  5. Article
  6. The heat is on: scaling improvements in photosynthetic thermal tolerance from the leaf to canopy to predict crop yields in a changing climate.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  7. Article
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  10. Article
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  12. Article
  13. Article
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  16. Article
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  18. Article
  19. Rubisco Activases: AAA+ Chaperones Adapted to Enzyme Repair.Frontiers in molecular biosciences · 2017
    Review
  20. 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

5 authors at 1 institution in 1 country.

Suratna HazraFrom the Department of Chemistry and Biochemistry and Center for Bioenergy and Photosynthesis, Arizona State University, Tempe, Arizona 85287.
J Nathan HendersonFrom the Department of Chemistry and Biochemistry and Center for Bioenergy and Photosynthesis, Arizona State University, Tempe, Arizona 85287.
Kevin LilesFrom the Department of Chemistry and Biochemistry and Center for Bioenergy and Photosynthesis, Arizona State University, Tempe, Arizona 85287.
Matthew T HiltonFrom the Department of Chemistry and Biochemistry and Center for Bioenergy and Photosynthesis, Arizona State University, Tempe, Arizona 85287.
Rebekka M WachterFrom the Department of Chemistry and Biochemistry and Center for Bioenergy and Photosynthesis, Arizona State University, Tempe, Arizona 85287 rwachter@asu.edu.
Arizona State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In many photosynthetic organisms, tight-binding Rubisco inhibitors are released by the motor protein Rubisco activase (Rca). In higher plants, Rca plays a pivotal role in regulating CO2 fixation. Here, the ATPase activity of 0.005 mm tobacco Rca was monitored under steady-state conditions, and global curve fitting was utilized to extract kinetic constants. The kcat was best fit by 22.3 ± 4.9 min(-1), the Km for ATP by 0.104 ± 0.024 mm, and the Ki for ADP by 0.037 ± 0.007 mm. Without ADP, the Hill coefficient for ATP hydrolysis was extracted to be 1.0 ± 0.1, indicating noncooperative behavior of homo-oligomeric Rca assemblies. However, the addition of ADP was shown to introduce positive cooperativity between two or more subunits (Hill coefficient 1.9 ± 0.2), allowing for regulation via the prevailing ATP/ADP ratio. ADP-mediated activation was not observed, although larger amounts led to competitive product inhibition of hydrolytic activity. The catalytic efficiency increased 8.4-fold upon cooperative binding of a second magnesium ion (Hill coefficient 2.5 ± 0.5), suggesting at least three conformational states (ATP-bound, ADP-bound, and empty) within assemblies containing an average of about six subunits. The addition of excess Rubisco (24:1, L8S8/Rca6) and crowding agents did not modify catalytic rates. However, high magnesium provided for thermal Rca stabilization. We propose that magnesium mediates the formation of closed hexameric toroids capable of high turnover rates and amenable to allosteric regulation. We suggest that in vivo, the Rca hydrolytic activity is tuned by fluctuating [Mg(2+)] in response to changes in available light.

Indexed as

Gene Expression Regulation, EnzymologicAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAllosteric SiteCatalysisCatalytic DomainChloroplastsGossypiumHydrolysisLightMagnesiumNADNicotianaOxidation-ReductionPhotosynthesisAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateMagnesiumNADRibulose-Bisphosphate CarboxylaseATPases associated with diverse cellular activities (AAA)carbon fixationchloroplastcooperativitymagnesium bindingmetal activationphotosynthesisproduct inhibitionRubisco regulationsite asymmetry

Identifiers

PMID26283786
PMCPMC4591810
OpenAlexW2255673426

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.