Evidence map›Paper›PMID 19513805›Full record

ArticlePlant molecular biology2009

Characterization of the wheat endosperm transfer cell-specific protein TaPR60.

Nataliya Kovalchuk, Jessica Smith, Margaret Pallotta, Rohan Singh, Ainur Ismagul, Serik Eliby, Natalia Bazanova, Andrew S Milligan, Maria Hrmova, Peter Langridge and 1 more

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Article in Plant molecular biology, 2009. 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
–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

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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.

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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

11 authors.

Nataliya KovalchukAustralian Centre for Plant Functional Genomics, Glen Osmond, SA 5064, Australia.
Jessica Smith
Margaret Pallotta
Rohan Singh
Ainur Ismagul
Serik Eliby
Natalia Bazanova
Andrew S Milligan
Maria Hrmova
Peter Langridge
Sergiy Lopato

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The TaPR60 gene from bread wheat encodes a small cysteine-rich protein with a hydrophobic signal peptide, predicted to direct the TaPR60 protein to a secretory pathway. It was demonstrated by heterologous expression of recombinant TaPR60 protein that the signal peptide is recognized and cleaved in yeast cells. The full-length gene including promoter sequence of a TaPR60 orthologue was cloned from a BAC library of Triticum durum. A transcriptional promoter-GUS fusion was stably transformed into wheat, barley and rice. The strongest GUS expression in wheat and barley was found in the endosperm transfer cells, while in rice the promoter was active inside the starchy endosperm during the early stages of grain filling. The TaPR60 gene was also used as bait in a yeast two-hybrid screen. Five proteins were identified in the screen, and for some of these prey proteins, the interaction was confirmed by co-immunoprecipitation. The signal peptide binding proteins, TaUbiL1 and TaUbiL2, are homologues of animal proteins, which belong to proteolytic complexes, and therefore may be responsible for TaPR60 processing or degradation of the signal peptide. Other proteins that interact with TaPR60 may have a function in TaPR60 secretion or regulation of this process. Examination of a three dimensional model of TaPR60 suggested that this protein could be involved in binding of lipidic molecules.

Indexed as

Amino Acid SequenceCloning, MolecularCodonHordeumMolecular Sequence DataOryzaProlaminsPromoter Regions, GeneticProtein BiosynthesisRhizobiumSequence AlignmentSequence Homology, Amino AcidTransformation, GeneticTriticumCodonProlamins

Identifiers

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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.