Evidence map›Paper›PMID 18390594›Full record

ArticleThe Plant cell2008

Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts upstream of three active beta-amylases in Arabidopsis chloroplasts.

Daniel C Fulton, Michaela Stettler, Tabea Mettler, Cara K Vaughan, Jing Li, Perigio Francisco, Manuel Gil, Heike Reinhold, Simona Eicke, Gaëlle Messerli and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed, 1 pooled it
11.2field-weighted citation impact, top 1% 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

160 citing papers in PubMed, 1 synthesis or guideline pooled it, 379 citations in OpenAlex.

  1. Pooled it
  2. Combined linkage mapping and association analysis reveal the genetic control of starch content in maize kernel.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Pangenome-assisted characterization of TaBAM genes and association of TaBAM16-1B with NDVI in wheat.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
    Article
  8. Article
  9. A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Horticulture research · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

100 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

15 authors at 5 institutions in 3 countries.

Daniel C FultonInstitute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JH, United Kingdom.
Michaela Stettler
Tabea Mettler
Cara K Vaughan
Jing Li
Perigio Francisco
Manuel Gil
Heike Reinhold
Simona Eicke
Gaëlle Messerli
Gary Dorken
Karen Halliday
Alison M Smith
Steven M Smith
Samuel C Zeeman
ETH Zurich · CHAustralian Research Council · AUUniversity of Edinburgh · GBBirkbeck, University of London · GBJohn Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council 15/D20100Biotechnology and Biological Sciences Research Council D20100
6 · The paper itself

Abstract

This work investigated the roles of beta-amylases in the breakdown of leaf starch. Of the nine beta-amylase (BAM)-like proteins encoded in the Arabidopsis thaliana genome, at least four (BAM1, -2, -3, and -4) are chloroplastic. When expressed as recombinant proteins in Escherichia coli, BAM1, BAM2, and BAM3 had measurable beta-amylase activity but BAM4 did not. BAM4 has multiple amino acid substitutions relative to characterized beta-amylases, including one of the two catalytic residues. Modeling predicts major differences between the glucan binding site of BAM4 and those of active beta-amylases. Thus, BAM4 probably lost its catalytic capacity during evolution. Total beta-amylase activity was reduced in leaves of bam1 and bam3 mutants but not in bam2 and bam4 mutants. The bam3 mutant had elevated starch levels and lower nighttime maltose levels than the wild type, whereas bam1 did not. However, the bam1 bam3 double mutant had a more severe phenotype than bam3, suggesting functional overlap between the two proteins. Surprisingly, bam4 mutants had elevated starch levels. Introduction of the bam4 mutation into the bam3 and bam1 bam3 backgrounds further elevated the starch levels in both cases. These data suggest that BAM4 facilitates or regulates starch breakdown and operates independently of BAM1 and BAM3. Together, our findings are consistent with the proposal that beta-amylase is a major enzyme of starch breakdown in leaves, but they reveal unexpected complexity in terms of the specialization of protein function.

Indexed as

Amino Acid SequenceArabidopsisBase Sequencebeta-AmylaseCatalysisChloroplastsDNA PrimersEscherichia coliMicroscopy, FluorescenceMolecular Sequence DataRecombinant ProteinsSequence Homology, Amino AcidStarchbeta-AmylaseDNA PrimersRecombinant ProteinsStarch

Identifiers

PMID18390594
PMCPMC2390740
OpenAlexW2121631499

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.