Evidence map›Paper›PMID 29260339›Full record

ArticleJournal of plant research2018

Molecular characterisation of two novel starch granule proteins 1 in wild and cultivated diploid A genome wheat species.

Ermelinda Botticella, Anna Pucci, Francesco Sestili

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Article in Journal of plant research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 80% of its field
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 2 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Ermelinda BotticellaDepartment of Agriculture and Forestry Sciences, University of Tuscia, Via S. Camillo de Lellis SNC, Viterbo, Italy.
Anna PucciDepartment of Agriculture and Forestry Sciences, University of Tuscia, Via S. Camillo de Lellis SNC, Viterbo, Italy.
Francesco SestiliDepartment of Agriculture and Forestry Sciences, University of Tuscia, Via S. Camillo de Lellis SNC, Viterbo, Italy. francescosestili@unitus.it.
Università degli Studi della Tuscia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Starch synthase IIa, also known as starch granule protein 1 (SGP-1), plays a key role in amylopectin biosynthesis. The absence of SGP-1 in cereal grains is correlated to dramatic changes in the grains' starch content, structure, and composition. An extensive investigation of starch granule proteins in this study revealed a polymorphism in the electrophoretic mobility of SGP-1 between two species of wheat, Triticum urartu and T. monococcum; this protein was, however, conserved among all other Triticum species that share the A genome inherited from their progenitor T. urartu. Two different electrophoretic profiles were identified: SGP-A1 proteins of T. urartu accessions had a SDS-PAGE mobility similar to those of tetraploid and hexaploid wheat species; conversely, SGP-A1 proteins of T. monococcum ssp. monococcum and ssp. boeoticum accessions showed a different electrophoretic mobility. The entire coding region of the two genes was isolated and sequenced in an attempt to explain the polymorphism identified. Several single nucleotide polymorphisms (SNPs) responsible for amino acid changes were identified, but no indel polymorphism was observed to explain the difference in electrophoretic mobility. Amylose content did not differ significantly among T. urartu, T. monococcum ssp. boeoticum and T. monococcum ssp. monococcum, except in one accession of the ssp. boeoticum. Conversely, several interspecific differences were observed in viscosity properties (investigated as viscosity profiles using a rapid visco analyzer-RVA profiles) of these cereal grains. T. monococcum ssp. boeoticum accessions had the lowest RVA profiles, T. urartu accessions had an intermediate RVA profile, whereas T. monococcum ssp. monococcum showed the highest RVA profile. These differences could be associated with the numerous amino acid and structural changes evident among the SGP-1 proteins.

Indexed as

DiploidyGenome, PlantModels, StructuralPhylogenyPlant ProteinsPoaceaePolymorphism, GeneticSequence Analysis, DNAStarchStarch SynthaseTriticumPlant ProteinsStarchStarch Synthasestarch synthase IIDiploid wheatGel shiftingPhylogenesisPolymorphismStarch granule proteinsStarch synthase

Identifiers

PMID29260339
OpenAlexW2779470341

What OpenQuestion holds

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Registered trials

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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.