Evidence map›Paper›PMID 16751439›Full record

ArticlePlant physiology2006

Molecular and structural characterization of hexameric beta-D-glucosidases in wheat and rye.

Masayuki Sue, Kana Yamazaki, Shunsuke Yajima, Taiji Nomura, Tetsuya Matsukawa, Hajime Iwamura, Toru Miyamoto

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The C-Domain of OleuropeinPlant physiology · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Delivering sustainable crop protection systems via the seed: exploiting natural constitutive and inducible defence pathways.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Review
  15. Article
  16. Article
  17. Article
  18. Dynamic reorganization of metabolic enzymes into intracellular bodies.Annual review of cell and developmental biology · 2012
    Review
  19. Article
  20. β-Glucosidases.Cellular and molecular life sciences : CMLS · 2010
    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

7 authors at 3 institutions in 1 country.

Masayuki SueDepartment of Applied Biology and Chemistry , Tokyo University of Agriculture, Setagaya, Tokyo 156-8502, Japan. sue@nodai.ac.jp
Kana Yamazaki
Shunsuke Yajima
Taiji Nomura
Tetsuya Matsukawa
Hajime Iwamura
Toru Miyamoto
Kyoto University · JPTokyo University of Agriculture · JPKindai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The wheat (Triticum aestivum) and rye (Secale cereale) beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, exist as different types of isozyme, and function as oligomers. In this study, three cDNAs encoding beta-D-glucosidases (TaGlu1a, TaGlu1b, and TaGlu1c) were isolated from young wheat shoots. Although the TaGlu1s share very high sequence homology, the mRNA level of Taglu1c was much lower than the other two genes in 48- and 96-h-old wheat shoots. The expression ratio of each gene was different between two wheat cultivars. Recombinant TaGlu1b expressed in Escherichia coli was electrophoretically distinct fromTaGlu1a and TaGlu1c. Furthermore, coexpression of TaGlu1a and TaGlu1b gave seven bands on a native-PAGE gel, indicating the formation of both homo- and heterohexamers. One distinctive property of the wheat and rye glucosidases is that they function as hexamers but lose activity when dissociated into smaller oligomers or monomers. The crystal structure of hexameric TaGlu1b was determined at a resolution of 1.8 A. The N-terminal region was located at the dimer-dimer interface and plays a crucial role in hexamer formation. Mutational analyses revealed that the aromatic side chain at position 378, which is located at the entrance to the catalytic center, plays an important role in substrate binding. Additionally, serine-464 and leucine-465 of TaGlu1a were shown to be critical in the relative specificity for DIMBOA-glucose (2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one) over DIBOA-glucose (7-demethoxy-DIMBOA-glucose).

Indexed as

Amino Acid SequenceBinding SitesCellulasesCrystallography, X-RayDimerizationDNA, ComplementaryElectrophoresis, Polyacrylamide GelEscherichia coliIsoenzymesModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPlant ProteinsProtein Structure, QuaternaryRecombinant Fusion ProteinsRNA, MessengerCellulasesDNA, ComplementaryIsoenzymesPlant ProteinsRecombinant Fusion ProteinsRNA, Messenger

Identifiers

PMID16751439
PMCPMC1533919
OpenAlexW2007024189

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.