Evidence map›Paper›PMID 42236489›Full record

ArticleNature communications2026

Diversity-driven biochemical survey reveals widespread dimerization throughout the rubisco superfamily.

Alexander J Kehl, Leah Taylor-Kearney, Alexander L Jaffe, Jose Henrique Pereira, Jennifer Lee, Michal Hammel, Lucas M Waldburger, Caroline Yeow, Luis Valentin-Alvarado, Paul D Adams and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors.

Alexander J Kehl *Biophysics Graduate Group, University of California, Davis, Davis, CA, USA.
Leah Taylor-Kearney *Environmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Alexander L JaffeDepartment of Earth System Science, Stanford University, Stanford, CA, USA.
Jose Henrique PereiraFeedstocks Division, Joint BioEnergy Institute, Emeryville, CA, USA.
Jennifer LeeGenome Center, University of California Davis, Davis, CA, USA.
Michal HammelMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-5610-9289
Lucas M WaldburgerEnvironmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Caroline YeowGenome Center, University of California Davis, Davis, CA, USA.
Luis Valentin-AlvaradoDepartment of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Australia.ORCID http://orcid.org/0000-0001-7988-8556
Paul D AdamsMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID http://orcid.org/0000-0001-9333-8219
Jillian F BanfieldInnovative Genomics Institute, University of California, Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0001-8203-8771
Justin B SiegelGenome Center, University of California Davis, Davis, CA, USA.
Noam PrywesDepartment of Biochemistry, University of Cambridge, Cambridge, UK. np648@cam.ac.uk.ORCID http://orcid.org/0000-0003-2526-2392
Patrick M ShihEnvironmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA. pmshih@berkeley.edu.ORCID http://orcid.org/0000-0002-2119-3345

Funding

U.S. Department of Energy (DOE) DE-AC02-05CH11231
6 · The paper itself

Abstract

Rubisco is the entry point of nearly all organic carbon into the biosphere and is present in all domains of life. Despite its global importance, biochemical studies of this enzyme superfamily have been limited to a relatively narrow set of subclades. Recent advances in metagenomics have dramatically reshaped our understanding of both microbial and rubisco diversity; however, biochemical characterization of these sequences has not kept pace with the exponential growth in sequence data. To better survey the functional and structural diversity of rubisco, we systematically sample and synthesize a library of diverse rubisco sequences with an emphasis on clades that are sparsely represented in the biochemical literature. Our updated phylogenetic analysis reveals that many deep‑branching rubiscos assemble as dimers, supporting a dimeric origin for the superfamily - in contrast to the ecologically dominant hexadecameric form I. Additionally, we discover and structurally characterize an unusually large catalytic subunit among characterized rubiscos, originating from a early-branching subclade with secondary structural elements not present in canonical rubisco architectures.

Indexed as

Protein MultimerizationRibulose-Bisphosphate CarboxylaseCatalytic DomainModels, MolecularPhylogenyRibulose-Bisphosphate Carboxylase

Identifiers

PMID42236489
PMCPMC13454268

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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.