Trafficking and deposition of prolamins in wheat

Tosi, Paola

doi:10.1016/j.jcs.2012.02.004

Cited by 36 publications

(28 citation statements)

References 99 publications

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“…There is a general consensus that wheat prolamins are transported to the protein storage vacuole by two different pathways: Golgi dependent and Golgi independent (Tosi, ). However, there is disagreement as to whether or not different prolamins are transported through the two routes differentially, and if so, what causes the difference (Levanony et al ., ; Loussert et al ., ; Rubin et al ., ; Tosi et al ., ).…”

Section: Discussionmentioning

confidence: 99%

Gluten quality of bread wheat is associated with activity of RabD GTPases

Tyler

Bhandari

Poole

et al. 2014

Plant Biotechnology Journal

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In the developing endosperm of bread wheat (Triticum aestivum), seed storage proteins are produced on the rough endoplasmic reticulum (ER) and transported to protein bodies, specialized vacuoles for the storage of protein. The functionally important gluten proteins of wheat are transported by two distinct routes to the protein bodies where they are stored: vesicles that bud directly off the ER and transport through the Golgi. However, little is known about the processing of glutenin and gliadin proteins during these steps or the possible impact on their properties. In plants, the RabD GTPases mediate ER-to-Golgi vesicle transport. Available sequence information for Rab GTPases in Arabidopsis, rice, Brachypodium and bread wheat was compiled and compared to identify wheat RabD orthologs. Partial genetic sequences were assembled using the first draft of the Chinese Spring wheat genome. A suitable candidate gene from the RabD clade (TaRabD2a) was chosen for down-regulation by RNA interference (RNAi), and an RNAi construct was used to transform wheat plants. All four available RabD genes were shown by qRT-PCR to be down-regulated in the transgenic developing endosperm. The transgenic grain was found to produce flour with significantly altered processing properties when measured by farinograph and extensograph. SE-HPLC found that a smaller proportion of HMW-GS and large proportion of LMW-GS are incorporated into the glutenin macropolymer in the transgenic dough. Lower protein content but a similar protein profile on SDS-PAGE was seen in the transgenic grain.

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Section: Discussionmentioning

confidence: 99%

Gluten quality of bread wheat is associated with activity of RabD GTPases

Tyler

Bhandari

Poole

et al. 2014

Plant Biotechnology Journal

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“…PINs contain a signal peptide similar to that of prolamins. It consists of 20 amino acids in total, with an internal stretch of at least 6 hydrophobic amino acids preceded by a short positively charged sequence (Tosi ). Finally, Lesage and others () and Meziani and others () did not detect any PINs in the aleurone layer, in contrast to what was found in the aforementioned studies (Dubreil and others ; Capparelli and others ).…”

Section: Wheat Puroindolines: Genetics Structure Occurrence and Bimentioning

confidence: 99%

Wheat (Triticum aestivum L. and T. turgidum L. ssp. durum) Kernel Hardness: I. Current View on the Role of Puroindolines and Polar Lipids

Pauly

Pareyt

Fierens

et al. 2013

Comp Rev Food Sci Food Safe

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Wheat hardness has major consequences for the entire wheat supply chain from breeders and millers over manufacturers to, finally, consumers of wheat-based products. Indeed, differences in hardness among Triticum aestivum L. or between T. aestivum L. and T. turgidum L. ssp. durum wheat cultivars determine not only their milling properties, but also the properties of flour or semolina endosperm particles, their preferential use in cereal-based applications, and the quality of the latter. Although the mechanism causing differences in wheat hardness has been subject of research more than once, it is still not completely understood. It is widely accepted that differences in wheat hardness originate from differences in the interaction between the starch granules and the endosperm protein matrix in the kernel. This interaction seems impacted by the presence of either puroindoline a and/or b, polar lipids on the starch granule surface, or by a combination of both. We focus here on wheat hardness and its relation to the presence of puroindolines and polar lipids. More in particular, the structure, properties, and genetics of puroindolines and their interactions with polar lipids are critically discussed as is their possible role in wheat hardness. We also address future research needs as well as the presence of puroindoline-type proteins in other cereals.

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“…5C, F), unlike in wild-type rice (see Supplementary Data Fig. S2), the integrity of the protein bodies appeared to be disrupted in some regions of the endosperm (mainly in the inner layers), suggesting that a process of protein matrix formation similar to that observed in wheat endosperm (Parker, 1980; Tosi et al , 2009; Tosi, 2012) may be occurring.…”

Section: Resultsmentioning

confidence: 87%

The trafficking pathway of a wheat storage protein in transgenic rice endosperm

Oszvald¹,

Tamás²,

Shewry³

et al. 2014

Annals of Botany

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Background and AimsThe trafficking of proteins in the endoplasmic reticulum (ER) of plant cells is a topic of considerable interest since this organelle serves as an entry point for proteins destined for other organelles, as well as for the ER itself. In the current work, transgenic rice was used to study the pattern and pathway of deposition of the wheat high molecular weight (HMW) glutenin sub-unit (GS) 1Dx5 within the rice endosperm using specific antibodies to determine whether it is deposited in the same or different protein bodies from the rice storage proteins, and whether it is located in the same or separate phases within these.MethodsThe protein distribution and the expression pattern of HMW sub-unit 1Dx5 in transgenic rice endosperm at different stages of development were determined using light and electron microscopy after labelling with antibodies.Key resultsThe use of HMW-GS-specific antibodies showed that sub-unit 1Dx5 was expressed mainly in the sub-aleurone cells of the endosperm and that it was deposited in both types of protein body present in the rice endosperm: derived from the ER and containing prolamins, and derived from the vacuole and containing glutelins. In addition, new types of protein bodies were also formed within the endosperm cells.ConclusionsThe results suggest that the HMW 1Dx5 protein could be trafficked by either the ER or vacuolar pathway, possibly depending on the stage of development, and that its accumulation in the rice endosperm could compromise the structural integrity of protein bodies and their segregation into two distinct populations in the mature endosperm.

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Trafficking and deposition of prolamins in wheat

Cited by 36 publications

References 99 publications

Gluten quality of bread wheat is associated with activity of RabD GTPases

Gluten quality of bread wheat is associated with activity of RabD GTPases

Wheat (Triticum aestivum L. and T. turgidum L. ssp. durum) Kernel Hardness: I. Current View on the Role of Puroindolines and Polar Lipids

The trafficking pathway of a wheat storage protein in transgenic rice endosperm

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