Evidence map›Paper›PMID 10412910›Full record

ArticlePlant molecular biology1999

A novel E-type endo-beta-1,4-glucanase with a putative cellulose-binding domain is highly expressed in ripening strawberry fruits.

L Trainotti, S Spolaore, A Pavanello, B Baldan, G Casadoro

Abstract read
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In one paragraph

Article in Plant molecular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
11.3field-weighted citation impact, top 2% 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

30 citing papers in PubMed, 120 citations in OpenAlex.

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  17. Biochemistry of fruit softening: an overview.Physiology and molecular biology of plants : an international journal of functional plant biology · 2009
    Article
  18. Article
  19. Carbohydrate binding modules: biochemical properties and novel applications.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  20. Article
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.

L TrainottiDipartimento di Biologia, Università di Padova, Italy.
S Spolaore
A Pavanello
B Baldan
G Casadoro
University of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two full-length cDNA clones (faEG1 and faEG3, respectively) have been isolated by screening a cDNA library representing transcripts from red strawberry fruits. Southern blot analysis of genomic DNA suggests that the strawberry endo-beta-1,4-glucanases (EGases) are encoded by a multigene family. The cognate genes are predominantly expressed during the ripening process proper, although, in the case of faEG3, some expression has also been observed in large green fruits and, at low amounts, in young vegetative green tissues. In agreement with other ripening-related genes in strawberry, also the expression of faEG1 and faEG3 is down-regulated by treatment with an auxin analogue (1-naphthaleneacetic acid, NAA). Differences in temporal expression of the two EGase genes in fruits are not accompanied by differences in spatial expression. The pattern of expression and the sequence characteristics of the two polypeptides suggest that the two strawberry EGases operate in a synergistic and coordinate manner. The protein encoded by faEG1 looks like one of the usual higher-plant EGases (average molecular mass of 54 kDa), while the protein encoded by faEG3 has a greater deduced molecular mass (about 68 kDa) due to the presence of an extra peptide of about 130 amino acids at the C-terminus. Such unusual peptide shows some features also found in microbial cellulases and contains a putative cellulose-binding domain. We propose that the faEG3-encoded EGase might especially hydrolyse the xyloglucans coating the cellulose microfibrils, thus rendering the cell wall more susceptible to the subsequent hydrolytic activity of the faEG1-encoded EGase.

Indexed as

Amino Acid SequenceBinding SitesCellulaseCelluloseDNA, ComplementaryFruitGene ExpressionGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicGene Expression Regulation, PlantIndoleacetic AcidsIn Situ HybridizationIsoenzymesMolecular Sequence DataRNASequence AlignmentCellulaseCelluloseDNA, ComplementaryIndoleacetic AcidsIsoenzymesRNA

Identifiers

PMID10412910
OpenAlexW318562260

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.