Evidence map›Paper›PMID 18063718›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2007

Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.

F Robert Tabita, Thomas E Hanson, Huiying Li, Sriram Satagopan, Jaya Singh, Sum Chan

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
5.8field-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

150 citing papers in PubMed, 389 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. On the emergence of metabolism: the evolution of proteins that powered life.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Cyanobacteria from marine oxygen-deficient zones encode both form I and form II Rubiscos.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Microorganisms · 2024
    Article
  18. Engineering Rubisco to enhance COSynthetic and systems biotechnology · 2024
    Review
  19. Article
  20. Article

90 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 4 institutions in 1 country.

F Robert TabitaDepartment of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210-1292, USA. Tabita.1@osu.edu
Thomas E Hanson
Huiying Li
Sriram Satagopan
Jaya Singh
Sum Chan
The Ohio State University · USHoward Hughes Medical Institute · USUniversity of California, Los Angeles · USUniversity of Delaware · US

Funding

FUNCTION AND ASSEMBLY OF CO2 ASSIMILATORY ENZYMESR01GM024497 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI TABITA, F ROBERT · 1985 to 2005
$1.2M
NIGMS NIH HHS GM24497NIGMS NIH HHS R01 GM024497
6 · The paper itself

Abstract

About 30 years have now passed since it was discovered that microbes synthesize RubisCO molecules that differ from the typical plant paradigm. RubisCOs of forms I, II, and III catalyze CO(2) fixation reactions, albeit for potentially different physiological purposes, while the RubisCO-like protein (RLP) (form IV RubisCO) has evolved, thus far at least, to catalyze reactions that are important for sulfur metabolism. RubisCO is the major global CO(2) fixation catalyst, and RLP is a somewhat related protein, exemplified by the fact that some of the latter proteins, along with RubisCO, catalyze similar enolization reactions as a part of their respective catalytic mechanisms. RLP in some organisms catalyzes a key reaction of a methionine salvage pathway, while in green sulfur bacteria, RLP plays a role in oxidative thiosulfate metabolism. In many organisms, the function of RLP is unknown. Indeed, there now appear to be at least six different clades of RLP molecules found in nature. Consideration of the many RubisCO (forms I, II, and III) and RLP (form IV) sequences in the database has subsequently led to a coherent picture of how these proteins may have evolved, with a form III RubisCO arising from the Methanomicrobia as the most likely ultimate source of all RubisCO and RLP lineages. In addition, structure-function analyses of RLP and RubisCO have provided information as to how the active sites of these proteins have evolved for their specific functions.

Indexed as

Amino Acid SequenceBacteriaBacterial ProteinsBiological EvolutionCarbon DioxideCatalysisMethionineModels, MolecularMolecular Sequence DataRibulose-Bisphosphate CarboxylaseSequence AlignmentStructure-Activity RelationshipBacterial ProteinsCarbon DioxideMethionineRibulose-Bisphosphate Carboxylase

Identifiers

PMID18063718
PMCPMC2168653
OpenAlexW2171866573

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.