Spectroscopic Characterisation of the Lipid-binding Properties of Wheat Puroindolines

Kooijman, M.; Orsel, R.; Hessing, M.; Hamer, R.J.; Bekkers, A.C.A.P.A.

doi:10.1006/jcrs.1997.0115

Cited by 51 publications

(65 citation statements)

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“…PINA isoforms with N-termini with and without Asp + 1 have been found (Blochet et al 1993;Ikeda et al 2005), as well as processing at 3, 4 or 5 residues at the C-terminus (Blochet et al 1993); similar processing is suggested for PINB . Kooijman et al (1997) failed to find N-terminal heterogeneity for either protein, but Day et al (2006) identified C-terminal polymorphic forms (with or without an Ile-Gly extension after the Thr) for PINA, and both N-terminal (with or without the first Glu) and C-terminal (with or without a Tyr-Tyr after the Ser-Gly) polymorphic forms for PINB in different cultivars, suggesting alternative processing and/or inter-varietal differences. The N-terminal cleavable peptide and C-terminal cleavable extensions are suggested to play a role in the intracellular targeting and functions of puroindolines .…”

Section: Biochemical Properties Of Puroindoline Proteinsmentioning

confidence: 67%

Molecular genetics of puroindolines and related genes: allelic diversity in wheat and other grasses

2007

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The hardness or texture of cereal grains is a primary determinant of their technological and processing quality. Among members of the Triticeae, most notably wheat, much of the variation in texture is controlled by a single locus comprised of the Puroindoline a, Puroindoline b and Grain Softness Protein-1 (Gsp-1) genes. Puroindolines confer the three major texture classes of soft and hard common wheat and the very hard durum wheat. The protein products of these genes interact with lipids and are associated with the surface of isolated starch (as a protein fraction known as 'friabilin'). During the past ten years a great diversity of alleles of both Puroindoline genes have been discovered and significant advances made in understanding the relationship between the gene presence/absence, sequence polymorphism and texture of cereal grains. Efforts have also focussed on Puroindoline and Gsp-1 genes in diploid progenitors, other Triticeae grasses and synthetic wheats in order to understand the evolution of this gene family and find potentially useful variants. The puroindoline homologues in other cereals such as rye and barley are also receiving attention. This work summarises new developments in molecular genetics of puroindolines in wheat and related Triticeae grasses, and the related genes in other cereals.

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Section: Biochemical Properties Of Puroindoline Proteinsmentioning

confidence: 67%

Molecular genetics of puroindolines and related genes: allelic diversity in wheat and other grasses

2007

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“…Due to the presence of the tryptophan-rich domain, puroindolines have also unique lipid-binding properties (23,26,27), which could be responsible for their antifungal activity (20,26). They also have good foaming properties and both PIN-a and PIN-b form highly stable foams even in the presence of lipids (23)(24)(25).…”

Section: Introductionmentioning

confidence: 99%

“…Puroindolines have interesting interfacial properties (23)(24)(25)(26)(27). Due to the presence of the tryptophan-rich domain, puroindolines have also unique lipid-binding properties (23,26,27), which could be responsible for their antifungal activity (20,26).…”

Section: Introductionmentioning

confidence: 99%

Interfacial Behavior of Wheat Puroindolines: Study of Adsorption at the Air–Water Interface from Surface Tension Measurement Using Wilhelmy Plate Method

Biswas

Dubreil

Marion

2001

Journal of Colloid and Interface Science

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“…They are puroindoline a (pinA), puroindoline b (pinB) and Gsp-1a. Puroindolines contain a tryptophan-rich region that appears to be involved in lipid binding (Kooijman et al 1997). The first evidence that puroindolines may be involved in grain hardness came in a publication by Greenwell and Schofield (1986).…”

Section: Introductionmentioning

confidence: 99%

Expression of wild-type pinB sequence in transgenic wheat complements a hard phenotype

et al. 2002

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Wheat grain hardness is a major factor in the wheat end-product quality. Grain hardness in wheat affects such parameters as milling yield, starch damage and baking properties. A single locus determines whether wheat is hard or soft textured. This locus, termed Hardness ( Ha), resides on the short arm of chromosome 5D. Sequence alterations in the tryptophan-rich proteins puroindoline a and b (PINA and PINB) are inseparably linked to hard textured grain, but their role in endosperm texture has been controversial. Here, we show that the pinB-D1b alteration, common in hard textured wheats, can be complemented by the expression of wild-type pinB-D1a in transformed plants. Transgenic wheat seeds expressing wild-type pinB were soft in phenotype, having greatly increased friabilin levels, and greatly decreased kernel hardness and damaged starch. These results indicate that the pinB-D1b alteration is most likely the causative Ha mutation in the majority of hard wheats.

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Spectroscopic Characterisation of the Lipid-binding Properties of Wheat Puroindolines

Cited by 51 publications

References 0 publications

Molecular genetics of puroindolines and related genes: allelic diversity in wheat and other grasses

Molecular genetics of puroindolines and related genes: allelic diversity in wheat and other grasses

Interfacial Behavior of Wheat Puroindolines: Study of Adsorption at the Air–Water Interface from Surface Tension Measurement Using Wilhelmy Plate Method

Expression of wild-type pinB sequence in transgenic wheat complements a hard phenotype

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